3gzq - Revision history

OCA at 07:14, 6 September 2023

OCA — Wed, 06 Sep 2023 07:14:11 GMT

←Older revision		Revision as of 07:14, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3gzq' size='340' side='right'caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3gzq' size='340' side='right'caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.401Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>~~</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gzo\|3gzo]]~~, ~~[[3gzp\|3gzp]]~~<~~/div></td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">SOD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [https://pdbe.org/3gzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [https://www.ebi.ac.uk/pdbsum/3gzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gzq 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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [https://pdbe.org/3gzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [https://www.ebi.ac.uk/pdbsum/3gzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gzq 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]]
Line 41:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Superoxide dismutase]]~~	+	[[Category: Galaleldeen A]]
-	[[Category: Galaleldeen, A]]	+	[[Category: Hart PJ]]
-	[[Category: Hart~~, P J~~]]	+	[[Category: Taylor AB]]
-	[[Category: Taylor~~, A B~~]]	+	[[Category: Whitson LJ]]
-	[[Category: Whitson~~, L J]]~~	+
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Amyotrophic lateral sclerosis]]~~	+
-	~~[[Category: Antioxidant]]~~	+
-	~~[[Category: Apo]]~~	+
-	~~[[Category: Copper]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Disulfide bond]]~~	+
-	~~[[Category: Human cu]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Ubl conjugation]]~~	+
-	~~[[Category: Zinc]]~~	+
-	~~[[Category: Zn superoxide dismutase~~]]	+

OCA at 11:53, 13 October 2021

OCA — Wed, 13 Oct 2021 11:53:25 GMT

←Older revision		Revision as of 11:53, 13 October 2021
Line 1:		Line 1:

	==HUMAN SOD1 A4V Metal-free Variant==		==HUMAN SOD1 A4V Metal-free Variant==
-	<StructureSection load='3gzq' size='340' side='right' caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>	+	<StructureSection load='3gzq' size='340' side='right'caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gzo\|3gzo]], [[3gzp\|3gzp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gzo\|3gzo]], [[3gzp\|3gzp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [~~http~~://pdbe.org/3gzq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3gzq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3gzq 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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [https://pdbe.org/3gzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [https://www.ebi.ac.uk/pdbsum/3gzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gzq 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]]
Line 36:		Line 36:

	==See Also==		==See Also==
-	*[[Superoxide ~~Dismutase~~\|Superoxide ~~Dismutase~~]]	+	*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 42:		Line 42:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
	[[Category: Galaleldeen, A]]		[[Category: Galaleldeen, A]]

OCA at 05:49, 7 December 2018

OCA — Fri, 07 Dec 2018 05:49:53 GMT

←Older revision		Revision as of 05:49, 7 December 2018
Line 1:		Line 1:
		+
	==HUMAN SOD1 A4V Metal-free Variant==		==HUMAN SOD1 A4V Metal-free Variant==
	<StructureSection load='3gzq' size='340' side='right' caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3gzq' size='340' side='right' caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [http://pdbe.org/3gzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [http://www.ebi.ac.uk/pdbsum/3gzq 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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [http://pdbe.org/3gzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [http://www.ebi.ac.uk/pdbsum/3gzq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gzq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/3gzq_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/3gzq_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: Taylor, A B]]		[[Category: Taylor, A B]]
	[[Category: Whitson, L J]]		[[Category: Whitson, L J]]
		+	[[Category: Acetylation]]
	[[Category: Amyotrophic lateral sclerosis]]		[[Category: Amyotrophic lateral sclerosis]]
	[[Category: Antioxidant]]		[[Category: Antioxidant]]
	[[Category: Apo]]		[[Category: Apo]]
		+	[[Category: Copper]]
		+	[[Category: Cytoplasm]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Disulfide bond]]		[[Category: Disulfide bond]]
Line 55:		Line 59:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
		+	[[Category: Ubl conjugation]]
		+	[[Category: Zinc]]
	[[Category: Zn superoxide dismutase]]		[[Category: Zn superoxide dismutase]]

OCA at 08:12, 8 February 2016

OCA — Mon, 08 Feb 2016 08:12:35 GMT

←Older revision		Revision as of 08:12, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3gzq' size='340' side='right' caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3gzq' size='340' side='right' caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gzo\|3gzo]], [[3gzp\|3gzp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gzo\|3gzo]], [[3gzp\|3gzp]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [http://www.ebi.ac.uk/pdbsum/3gzq 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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [http://pdbe.org/3gzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [http://www.ebi.ac.uk/pdbsum/3gzq PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 22:
	<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=3gzq ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 32:		Line 32:
	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 3gzq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 40:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
	[[Category: Galaleldeen, A]]		[[Category: Galaleldeen, A]]

OCA at 17:49, 18 December 2014

OCA — Thu, 18 Dec 2014 17:49:59 GMT

←Older revision		Revision as of 17:49, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3gzq~~\| ~~PDB~~=3gzq \| ~~SCENE~~= }}	+	==HUMAN SOD1 A4V Metal-free Variant==
-	===~~HUMAN~~ SOD1 ~~A4V Metal~~-~~free Variant~~===	+	<StructureSection load='3gzq' size='340' side='right' caption='[[3gzq]], [[Resolution\|resolution]] 1.40Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19800308}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3gzq]] 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=3GZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GZQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3gzo\|3gzo]], [[3gzp\|3gzp]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3gzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gzq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gzq RCSB], [http://www.ebi.ac.uk/pdbsum/3gzq 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/gz/3gzq_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 ==
		+	Amyotrophic lateral sclerosis (ALS) is a fatal, progressive neurodegenerative disease characterized by the destruction of motor neurons in the spinal cord and brain. A subset of ALS cases are linked to dominant mutations in copper-zinc superoxide dismutase (SOD1). The pathogenic SOD1 variants A4V and G93A have been the foci of multiple studies aimed at understanding the molecular basis for SOD1-linked ALS. The A4V variant is responsible for the majority of familial ALS cases in North America, causing rapidly progressing paralysis once symptoms begin and the G93A SOD1 variant is overexpressed in often studied murine models of the disease. Here we report the three-dimensional structures of metal-free A4V and of metal-bound and metal-free G93A SOD1. In the metal-free structures, the metal-binding loop elements are observed to be severely disordered, suggesting that these variants may share mechanisms of aggregation proposed previously for other pathogenic SOD1 proteins.

-	~~==Disease==~~	+	Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.,Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ Arch Biochem Biophys. 2009 Dec;492(1-2):40-7. Epub 2009 Oct 1. PMID:19800308<ref>PMID:19800308</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==~~	+
-	~~[[3gzq]] 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=3GZQ OCA].~~	+

	==See Also==		==See Also==
	*[[Superoxide Dismutase\|Superoxide Dismutase]]		*[[Superoxide Dismutase\|Superoxide Dismutase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019800308</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
-	[[Category: Galaleldeen, A.]]	+	[[Category: Galaleldeen, A]]
-	[[Category: Hart, P J.]]	+	[[Category: Hart, P J]]
-	[[Category: Taylor, A B.]]	+	[[Category: Taylor, A B]]
-	[[Category: Whitson, L J.]]	+	[[Category: Whitson, L J]]
	[[Category: Amyotrophic lateral sclerosis]]		[[Category: Amyotrophic lateral sclerosis]]
	[[Category: Antioxidant]]		[[Category: Antioxidant]]

OCA at 07:03, 25 March 2013

OCA — Mon, 25 Mar 2013 07:03:42 GMT

←Older revision		Revision as of 07:03, 25 March 2013
Line 1:		Line 1:
-	[[Image:3gzq.png\|left\|200px]]
-
	{{STRUCTURE_3gzq\| PDB=3gzq \| SCENE= }}		{{STRUCTURE_3gzq\| PDB=3gzq \| SCENE= }}
-
	===HUMAN SOD1 A4V Metal-free Variant===		===HUMAN SOD1 A4V Metal-free Variant===
		+	{{ABSTRACT_PUBMED_19800308}}

-	~~{{ABSTRACT_PUBMED_19800308}}~~	+	==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:019800308</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019800308</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]

OCA at 09:30, 20 October 2012

OCA — Sat, 20 Oct 2012 09:30:33 GMT

←Older revision		Revision as of 09:30, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3gzq]] 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=3GZQ OCA].	+	[[3gzq]] 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=3GZQ OCA].

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

OCA: Protected "3gzq" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 23:05:27 GMT

Protected "3gzq" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:05, 25 July 2012

OCA at 23:05, 25 July 2012

OCA — Wed, 25 Jul 2012 23:05:26 GMT

←Older revision		Revision as of 23:05, 25 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3gzq.png\|left\|200px]]		[[Image:3gzq.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3gzq", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3gzq\| PDB=3gzq \| SCENE= }}		{{STRUCTURE_3gzq\| PDB=3gzq \| SCENE= }}

	===HUMAN SOD1 A4V Metal-free Variant===		===HUMAN SOD1 A4V Metal-free Variant===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19800308}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19800308 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19800308}}		{{ABSTRACT_PUBMED_19800308}}
-
-	==Disease==
-	Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147450 147450]]

	==About this Structure==		==About this Structure==
-	~~3GZQ~~ is a 2 ~~chains~~ structure of ~~sequences~~ 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=3GZQ OCA].	+	[[3gzq]] 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=3GZQ OCA].
		+
		+	==See Also==
		+	*[[Superoxide Dismutase\|Superoxide Dismutase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19800308~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019800308</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
Line 33:		Line 21:
	[[Category: Taylor, A B.]]		[[Category: Taylor, A B.]]
	[[Category: Whitson, L J.]]		[[Category: Whitson, L J.]]
-	[[Category: Acetylation]]
	[[Category: Amyotrophic lateral sclerosis]]		[[Category: Amyotrophic lateral sclerosis]]
	[[Category: Antioxidant]]		[[Category: Antioxidant]]
	[[Category: Apo]]		[[Category: Apo]]
-	[[Category: Copper]]
-	[[Category: Cytoplasm]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Disulfide bond]]		[[Category: Disulfide bond]]
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	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Ubl conjugation]]
-	[[Category: Zinc]]
	[[Category: Zn superoxide dismutase]]		[[Category: Zn superoxide dismutase]]
-
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OCA at 07:02, 23 December 2009

OCA — Wed, 23 Dec 2009 07:02:42 GMT

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-	[[Image:3gzq.~~jpg~~\|left\|200px]]	+	[[Image:3gzq.png\|left\|200px]]

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