2c9v - Revision history

OCA at 14:10, 13 December 2023

2023-12-13T14:10:49Z

←Older revision		Revision as of 14:10, 13 December 2023
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	<StructureSection load='2c9v' size='340' side='right'caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>		<StructureSection load='2c9v' size='340' side='right'caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9V FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.07Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [https://pdbe.org/2c9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [https://www.ebi.ac.uk/pdbsum/2c9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9v ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [https://pdbe.org/2c9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [https://www.ebi.ac.uk/pdbsum/2c9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[https://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>	+	[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[https://omim.org/entry/105400 105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.	+	[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Superoxide dismutase]]~~	+	[[Category: Antonyuk SV]]
-	[[Category: Antonyuk~~, S V~~]]	+	[[Category: Doucette PA]]
-	[[Category: Doucette~~, P A~~]]	+	[[Category: Hasnain SS]]
-	[[Category: Hasnain~~, S S~~]]	+	[[Category: Hough MA]]
-	[[Category: Hough~~, M A~~]]	+	[[Category: Strange RW]]
-	[[Category: Strange~~, R W~~]]	+	[[Category: Valentine JS]]
-	[[Category: Valentine~~, J S]]~~	+
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Amyotrophic lateral sclerosis]]~~	+
-	~~[[Category: Antioxidant]]~~	+
-	~~[[Category: Copper]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Human cu]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxioreductase]]~~	+
-	~~[[Category: Zinc]]~~	+
-	~~[[Category: Zn superoxide dismutase~~]]	+

OCA at 06:51, 1 December 2021

2021-12-01T06:51:23Z

OCA at 10:54, 26 February 2020

2020-02-26T10:54:39Z

←Older revision		Revision as of 10:54, 26 February 2020
Line 1:		Line 1:

	==Atomic resolution structure of Cu-Zn Human Superoxide dismutase==		==Atomic resolution structure of Cu-Zn Human Superoxide dismutase==
-	<StructureSection load='2c9v' size='340' side='right' caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>	+	<StructureSection load='2c9v' size='340' side='right'caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>
Line 34:		Line 34:

	==See Also==		==See Also==
-	*[[Superoxide ~~Dismutase~~\|Superoxide ~~Dismutase~~]]	+	*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
	[[Category: Antonyuk, S V]]		[[Category: Antonyuk, S V]]

OCA at 08:14, 23 May 2018

2018-05-23T08:14:34Z

←Older revision		Revision as of 08:14, 23 May 2018
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-	==~~ATOMIC RESOLUTION STRUCTURE OF CU~~-~~ZN HUMAN SUPEROXIDE DISMUTASE~~==	+
		+	==Atomic resolution structure of Cu-Zn Human Superoxide dismutase==
	<StructureSection load='2c9v' size='340' side='right' caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>		<StructureSection load='2c9v' size='340' side='right' caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://pdbe.org/2c9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://pdbe.org/2c9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 16:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9v_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9v_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 46:		Line 47:
	[[Category: Strange, R W]]		[[Category: Strange, R W]]
	[[Category: Valentine, J S]]		[[Category: Valentine, J S]]
		+	[[Category: Acetylation]]
	[[Category: Amyotrophic lateral sclerosis]]		[[Category: Amyotrophic lateral sclerosis]]
	[[Category: Antioxidant]]		[[Category: Antioxidant]]
		+	[[Category: Copper]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Human cu]]		[[Category: Human cu]]
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	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Oxioreductase]]		[[Category: Oxioreductase]]
		+	[[Category: Zinc]]
	[[Category: Zn superoxide dismutase]]		[[Category: Zn superoxide dismutase]]

OCA at 18:30, 7 February 2016

2016-02-07T18:30:51Z

←Older revision		Revision as of 18:30, 7 February 2016
Line 20:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c9v ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:04, 10 September 2015

2015-09-10T04:04:08Z

←Older revision		Revision as of 04:04, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2c9v' size='340' side='right' caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>		<StructureSection load='2c9v' size='340' side='right' caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://pdbe.org/2c9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2c9v" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
	[[Category: Antonyuk, S V]]		[[Category: Antonyuk, S V]]

OCA at 16:28, 15 January 2015

2015-01-15T16:28:12Z

←Older revision		Revision as of 16:28, 15 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>		<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>		[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
Line 39:		Line 39:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
-	[[Category: Antonyuk, S V.]]	+	[[Category: Antonyuk, S V]]
-	[[Category: Doucette, P A.]]	+	[[Category: Doucette, P A]]
-	[[Category: Hasnain, S S.]]	+	[[Category: Hasnain, S S]]
-	[[Category: Hough, M A.]]	+	[[Category: Hough, M A]]
-	[[Category: Strange, R W.]]	+	[[Category: Strange, R W]]
-	[[Category: Valentine, J S.]]	+	[[Category: Valentine, J S]]
	[[Category: Amyotrophic lateral sclerosis]]		[[Category: Amyotrophic lateral sclerosis]]
	[[Category: Antioxidant]]		[[Category: Antioxidant]]

OCA at 00:02, 30 September 2014

2014-09-30T00:02:36Z

←Older revision		Revision as of 00:02, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2c9v\| PDB=2c9v \| SCENE= }}~~	+	==ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE==
-	===ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE===	+	<StructureSection load='2c9v' size='340' side='right' caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>
-	~~{{ABSTRACT_PUBMED_16406071}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9V FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [http://www.ebi.ac.uk/pdbsum/2c9v PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9v_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human Cu-Zn superoxide dismutase (SOD1) protects cells from the effects of oxidative stress. Mutations in SOD1 are linked to the familial form of amyotrophic lateral sclerosis. Several hypotheses for their toxicity involve the mis-metallation of the enzyme. We present atomic-resolution crystal structures and biophysical data for human SOD1 in three metallation states: Zn-Zn, Cu-Zn and as-isolated. These data represent the first atomic-resolution structures for human SOD1, the first structure of a reduced SOD1, and the first structure of a fully Zn-substituted SOD1 enzyme. Recombinantly expressed as-isolated SOD1 contains a mixture of Zn and Cu at the Cu-binding site. The Zn-Zn structure appears to be at least as stable as the correctly (Cu-Zn) metallated enzyme. These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone.

-	~~==Disease==~~	+	Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes.,Strange RW, Antonyuk SV, Hough MA, Doucette PA, Valentine JS, Hasnain SS J Mol Biol. 2006 Mar 10;356(5):1152-62. Epub 2005 Dec 12. PMID:16406071<ref>PMID:16406071</ref>
-	~~[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause~~ of ~~amyotrophic lateral sclerosis type 1 (ALS1) [MIM~~:~~[http://omim.org/entry/105400 105400]]. ALS1 is a familial form~~ of ~~amyotrophic lateral sclerosis~~, ~~a neurodegenerative disorder affecting upper~~ and ~~lower motor neurons and resulting in fatal paralysis~~. ~~Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial~~, ~~involving both genetic and environmental factors~~. ~~The disease is inherited in~~ 5-~~10% of cases leading to familial forms~~.~~<ref>~~PMID:12963370</ref><ref>PMID:19741096</ref><ref>PMID:8528216</ref><ref>PMID:8682505</ref><ref>PMID:9541385</ref><ref>PMID:12754496</ref><ref>PMID:15056757</ref><ref>PMID:18378676</ref>[:]<ref>PMID:8446170</ref><ref>PMID:8351519</ref><ref>PMID:8179602</ref><ref>PMID:7980516</ref><ref>PMID:8069312</ref><ref>PMID:7951252</ref><ref>PMID:7881433</ref><ref>PMID:7836951</ref><ref>PMID:7997024</ref><ref>PMID:7870076</ref><ref>PMID:7887412</ref><ref>PMID:7795609</ref><ref>PMID:7655468</ref><ref>PMID:7655469</ref><ref>PMID:7655471</ref><ref>PMID:7700376</ref><ref>PMID:7647793</ref><ref>PMID:7501156</ref><ref>PMID:7496169</ref><ref>PMID:8938700</ref><ref>PMID:8907321</ref><ref>PMID:8990014</ref><ref>PMID:9101297</ref><ref>PMID:9455977</ref><ref>PMID:10732812</ref><ref>PMID:9131652</ref><ref>PMID:10400992</ref><ref>PMID:10430435</ref><ref>PMID:11535232</ref><ref>PMID:11369193</ref><ref>PMID:12402272</ref><ref>PMID:12145308</ref><ref>PMID:14506936</ref><ref>PMID:18552350</ref><ref>PMID:18301754</ref><ref>PMID:21247266</ref><ref>PMID:~~21220647~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[2c9v]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA].~~	+

	==See Also==		==See Also==
	*[[Superoxide Dismutase\|Superoxide Dismutase]]		*[[Superoxide Dismutase\|Superoxide Dismutase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:016406071</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]

OCA at 23:03, 24 March 2013

2013-03-24T23:03:27Z

←Older revision		Revision as of 23:03, 24 March 2013
Line 1:		Line 1:
-	[[Image:2c9v.png\|left\|200px]]
-
	{{STRUCTURE_2c9v\| PDB=2c9v \| SCENE= }}		{{STRUCTURE_2c9v\| PDB=2c9v \| SCENE= }}
-
	===ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE===		===ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE===
		+	{{ABSTRACT_PUBMED_16406071}}

-	~~{{ABSTRACT_PUBMED_16406071}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref><ref>PMID:19741096</ref><ref>PMID:8528216</ref><ref>PMID:8682505</ref><ref>PMID:9541385</ref><ref>PMID:12754496</ref><ref>PMID:15056757</ref><ref>PMID:18378676</ref>[:]<ref>PMID:8446170</ref><ref>PMID:8351519</ref><ref>PMID:8179602</ref><ref>PMID:7980516</ref><ref>PMID:8069312</ref><ref>PMID:7951252</ref><ref>PMID:7881433</ref><ref>PMID:7836951</ref><ref>PMID:7997024</ref><ref>PMID:7870076</ref><ref>PMID:7887412</ref><ref>PMID:7795609</ref><ref>PMID:7655468</ref><ref>PMID:7655469</ref><ref>PMID:7655471</ref><ref>PMID:7700376</ref><ref>PMID:7647793</ref><ref>PMID:7501156</ref><ref>PMID:7496169</ref><ref>PMID:8938700</ref><ref>PMID:8907321</ref><ref>PMID:8990014</ref><ref>PMID:9101297</ref><ref>PMID:9455977</ref><ref>PMID:10732812</ref><ref>PMID:9131652</ref><ref>PMID:10400992</ref><ref>PMID:10430435</ref><ref>PMID:11535232</ref><ref>PMID:11369193</ref><ref>PMID:12402272</ref><ref>PMID:12145308</ref><ref>PMID:14506936</ref><ref>PMID:18552350</ref><ref>PMID:18301754</ref><ref>PMID:21247266</ref><ref>PMID:21220647</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:016406071</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016406071</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]

OCA at 07:31, 20 October 2012

2012-10-20T07:31:33Z

←Older revision		Revision as of 07:31, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2c9v]] is a 2 chain structure ~~of [[Superoxide Dismutase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA].	+	[[2c9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA].

	==See Also==		==See Also==

←Older revision		Revision as of 06:51, 1 December 2021
Line 3:		Line 3:
	<StructureSection load='2c9v' size='340' side='right'caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>		<StructureSection load='2c9v' size='340' side='right'caption='[[2c9v]], [[Resolution\|resolution]] 1.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2C9V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9V FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1azv\|1azv]], [[1ba9\|1ba9]], [[1dsw\|1dsw]], [[1fun\|1fun]], [[1hl4\|1hl4]], [[1hl5\|1hl5]], [[1kmg\|1kmg]], [[1l3n\|1l3n]], [[1mfm\|1mfm]], [[1n18\|1n18]], [[1n19\|1n19]], [[1oez\|1oez]], [[1ozt\|1ozt]], [[1ozu\|1ozu]], [[1p1v\|1p1v]], [[1ptz\|1ptz]], [[1pu0\|1pu0]], [[1rk7\|1rk7]], [[1sos\|1sos]], [[1spd\|1spd]], [[1uxl\|1uxl]], [[1uxm\|1uxm]], [[2af2\|2af2]], [[2c9s\|2c9s]], [[2c9u\|2c9u]], [[4sod\|4sod]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [~~http~~://pdbe.org/2c9v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2c9v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9v ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9v OCA], [https://pdbe.org/2c9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9v RCSB], [https://www.ebi.ac.uk/pdbsum/2c9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[~~http~~://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>	+	[[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[https://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.	+	[[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]