4b3e - Revision history

OCA at 11:42, 20 December 2023

2023-12-20T11:42:16Z

←Older revision		Revision as of 11:42, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='4b3e' size='340' side='right'caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4b3e' size='340' side='right'caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B3E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B3E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.15Å</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]], [[2c9v\|2c9v]], [[2v0a\|2v0a]], [[2vr6\|2vr6]], [[2vr7\|2vr7]], [[2vr8\|2vr8]], [[2wko\|2wko]], [[2wyt\|2wyt]], [[2wyz\|2wyz]], [[2wz0\|2wz0]], [[2wz5\|2wz5]], [[2wz6\|2wz6]], [[2xjk\|2xjk]], [[2xjl\|2xjl]], [[4a7g\|4a7g]], [[4a7q\|4a7q]], [[4a7r\|4a7r]], [[4a7s\|4a7s]], [[4a7t\|4a7t]], [[4a7u\|4a7u]], [[4a7v\|4a7v]], [[4sod\|4sod]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [https://pdbe.org/4b3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [https://www.ebi.ac.uk/pdbsum/4b3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3e 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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [https://pdbe.org/4b3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [https://www.ebi.ac.uk/pdbsum/4b3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3e 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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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: Hasnain SS]]
-	[[Category: Hasnain~~, S S~~]]	+	[[Category: Hough MA]]
-	[[Category: Hough~~, M A~~]]	+	[[Category: Strange RW]]
-	[[Category: Strange~~, R W]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 06:58, 31 August 2022

2022-08-31T06:58:23Z

←Older revision		Revision as of 06:58, 31 August 2022
Line 3:		Line 3:
	<StructureSection load='4b3e' size='340' side='right'caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4b3e' size='340' side='right'caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4B3E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B3E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]], [[2c9v\|2c9v]], [[2v0a\|2v0a]], [[2vr6\|2vr6]], [[2vr7\|2vr7]], [[2vr8\|2vr8]], [[2wko\|2wko]], [[2wyt\|2wyt]], [[2wyz\|2wyz]], [[2wz0\|2wz0]], [[2wz5\|2wz5]], [[2wz6\|2wz6]], [[2xjk\|2xjk]], [[2xjl\|2xjl]], [[4a7g\|4a7g]], [[4a7q\|4a7q]], [[4a7r\|4a7r]], [[4a7s\|4a7s]], [[4a7t\|4a7t]], [[4a7u\|4a7u]], [[4a7v\|4a7v]], [[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]], [[2c9v\|2c9v]], [[2v0a\|2v0a]], [[2vr6\|2vr6]], [[2vr7\|2vr7]], [[2vr8\|2vr8]], [[2wko\|2wko]], [[2wyt\|2wyt]], [[2wyz\|2wyz]], [[2wz0\|2wz0]], [[2wz5\|2wz5]], [[2wz6\|2wz6]], [[2xjk\|2xjk]], [[2xjl\|2xjl]], [[4a7g\|4a7g]], [[4a7q\|4a7q]], [[4a7r\|4a7r]], [[4a7s\|4a7s]], [[4a7t\|4a7t]], [[4a7u\|4a7u]], [[4a7v\|4a7v]], [[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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [~~http~~://pdbe.org/4b3e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4b3e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3e 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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [https://pdbe.org/4b3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [https://www.ebi.ac.uk/pdbsum/4b3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3e 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:

	==See Also==		==See Also==
-	*[[Superoxide ~~Dismutase~~\|Superoxide ~~Dismutase~~]]	+	*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:23, 13 March 2019

2019-03-13T13:23:56Z

←Older revision		Revision as of 13:23, 13 March 2019
Line 1:		Line 1:

	==Structure of copper-zinc superoxide dismutase complexed with bicarbonate.==		==Structure of copper-zinc superoxide dismutase complexed with bicarbonate.==
-	<StructureSection load='4b3e' size='340' side='right' caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='4b3e' size='340' side='right'caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B3E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B3E FirstGlance]. <br>
Line 30:		Line 30:
	</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 01:48, 5 August 2016

2016-08-05T01:48:48Z

←Older revision		Revision as of 01:48, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of copper-zinc superoxide dismutase complexed with bicarbonate.==		==Structure of copper-zinc superoxide dismutase complexed with bicarbonate.==
	<StructureSection load='4b3e' size='340' side='right' caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4b3e' size='340' side='right' caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B3E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B3E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]], [[2c9v\|2c9v]], [[2v0a\|2v0a]], [[2vr6\|2vr6]], [[2vr7\|2vr7]], [[2vr8\|2vr8]], [[2wko\|2wko]], [[2wyt\|2wyt]], [[2wyz\|2wyz]], [[2wz0\|2wz0]], [[2wz5\|2wz5]], [[2wz6\|2wz6]], [[2xjk\|2xjk]], [[2xjl\|2xjl]], [[4a7g\|4a7g]], [[4a7q\|4a7q]], [[4a7r\|4a7r]], [[4a7s\|4a7s]], [[4a7t\|4a7t]], [[4a7u\|4a7u]], [[4a7v\|4a7v]], [[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]], [[2c9v\|2c9v]], [[2v0a\|2v0a]], [[2vr6\|2vr6]], [[2vr7\|2vr7]], [[2vr8\|2vr8]], [[2wko\|2wko]], [[2wyt\|2wyt]], [[2wyz\|2wyz]], [[2wz0\|2wz0]], [[2wz5\|2wz5]], [[2wz6\|2wz6]], [[2xjk\|2xjk]], [[2xjl\|2xjl]], [[4a7g\|4a7g]], [[4a7q\|4a7q]], [[4a7r\|4a7r]], [[4a7s\|4a7s]], [[4a7t\|4a7t]], [[4a7u\|4a7u]], [[4a7v\|4a7v]], [[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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [http://www.ebi.ac.uk/pdbsum/4b3e 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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [http://pdbe.org/4b3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [http://www.ebi.ac.uk/pdbsum/4b3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3e ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 4b3e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	__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 09:26, 21 December 2014

2014-12-21T09:26:23Z

←Older revision		Revision as of 09:26, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4b3e\| PDB=4b3e \| SCENE= }}~~	+	==Structure of copper-zinc superoxide dismutase complexed with bicarbonate.==
-	===Structure of copper-zinc superoxide dismutase complexed with bicarbonate.===	+	<StructureSection load='4b3e' size='340' side='right' caption='[[4b3e]], [[Resolution\|resolution]] 2.15Å' scene=''>
-	~~{{ABSTRACT_PUBMED_22984565}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4b3e]] is a 10 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=4B3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B3E FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]], [[2c9v\|2c9v]], [[2v0a\|2v0a]], [[2vr6\|2vr6]], [[2vr7\|2vr7]], [[2vr8\|2vr8]], [[2wko\|2wko]], [[2wyt\|2wyt]], [[2wyz\|2wyz]], [[2wz0\|2wz0]], [[2wz5\|2wz5]], [[2wz6\|2wz6]], [[2xjk\|2xjk]], [[2xjl\|2xjl]], [[4a7g\|4a7g]], [[4a7q\|4a7q]], [[4a7r\|4a7r]], [[4a7s\|4a7s]], [[4a7t\|4a7t]], [[4a7u\|4a7u]], [[4a7v\|4a7v]], [[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='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=4b3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b3e RCSB], [http://www.ebi.ac.uk/pdbsum/4b3e 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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Copper-zinc superoxide dismutase (SOD) is of fundamental importance to our understanding of oxidative damage. Its primary function is catalysing the dismutation of superoxide to O(2) and H(2)O(2). SOD also reacts with H(2)O(2), leading to the formation of a strong copper-bound oxidant species that can either inactivate the enzyme or oxidise other substrates. In the presence of bicarbonate (or CO(2)) and H(2)O(2), this peroxidase activity is enhanced and produces the carbonate radical. This freely diffusible reactive oxygen species is proposed as the agent for oxidation of large substrates that are too bulky to enter the active site. Here, we provide direct structural evidence, from a 2.15 A resolution crystal structure, of (bi)carbonate captured at the active site of reduced SOD, consistent with the view that a bound carbonate intermediate could be formed, producing a diffusible carbonate radical upon reoxidation of copper. The bound carbonate blocks direct access of substrates to Cu(I), suggesting that an adjunct to the accepted mechanism of SOD catalysed dismutation of superoxide operates, with Cu(I) oxidation by superoxide being driven via a proton-coupled electron transfer mechanism involving the bound carbonate rather than the solvent. Carbonate is captured in a different site when SOD is oxidised, being located in the active site channel adjacent to the catalytically important Arg143. This is the probable route of diffusion from the active site following reoxidation of the copper. In this position, the carbonate is poised for re-entry into the active site and binding to the reduced copper.

-	~~==Disease==~~	+	Structural evidence for a copper-bound carbonate intermediate in the peroxidase and dismutase activities of superoxide dismutase.,Strange RW, Hough MA, Antonyuk SV, Hasnain SS PLoS One. 2012;7(9):e44811. Epub 2012 Sep 11. PMID:22984565<ref>PMID:22984565</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==~~	+
-	~~[[4b3e]] is a 10 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=4B3E OCA].~~	+

	==See Also==		==See Also==
	*[[Superoxide Dismutase\|Superoxide Dismutase]]		*[[Superoxide Dismutase\|Superoxide Dismutase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
-	[[Category: Antonyuk, S V.]]	+	[[Category: Antonyuk, S V]]
-	[[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: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 06:46, 25 March 2013

2013-03-25T06:46:52Z

←Older revision		Revision as of 06:46, 25 March 2013
Line 1:		Line 1:
-	[[Image:4b3e.jpg\|left\|200px]]
-
	{{STRUCTURE_4b3e\| PDB=4b3e \| SCENE= }}		{{STRUCTURE_4b3e\| PDB=4b3e \| SCENE= }}
-
	===Structure of copper-zinc superoxide dismutase complexed with bicarbonate.===		===Structure of copper-zinc superoxide dismutase complexed with bicarbonate.===
-
	{{ABSTRACT_PUBMED_22984565}}		{{ABSTRACT_PUBMED_22984565}}
		+
		+	==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==
	[[4b3e]] is a 10 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=4B3E OCA].		[[4b3e]] is a 10 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=4B3E OCA].
		+
		+	==See Also==
		+	*[[Superoxide Dismutase\|Superoxide Dismutase]]
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]

OCA at 20:39, 26 September 2012

2012-09-26T20:39:34Z

←Older revision		Revision as of 20:39, 26 September 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4b3e.jpg\|left\|200px]]

-	~~The entry~~ 4b3e ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4b3e\| PDB=4b3e \| SCENE= }}

-	~~Authors: Strange, R.W., Hough, M.A., Antonyuk, S.V., Hasnain, S.S~~.	+	===Structure of copper-zinc superoxide dismutase complexed with bicarbonate.===

-	~~Description:~~ Structure ~~of copper~~-~~zinc superoxide~~ dismutase ~~complexed with bicarbonate~~.	+	{{ABSTRACT_PUBMED_22984565}}
		+
		+	==About this Structure==
		+	[[4b3e]] is a 10 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=4B3E OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Superoxide dismutase]]
		+	[[Category: Antonyuk, S V.]]
		+	[[Category: Hasnain, S S.]]
		+	[[Category: Hough, M A.]]
		+	[[Category: Strange, R W.]]
		+	[[Category: Oxidoreductase]]

OCA: Protected "4b3e" [edit=sysop:move=sysop]

2012-08-01T05:18:26Z

Protected "4b3e" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:18, 1 August 2012

OCA: New page: '''Unreleased structure''' The entry 4b3e is ON HOLD until Paper Publication Authors: Strange, R.W., Hough, M.A., Antonyuk, S.V., Hasnain, S.S. Description: Structure of copper-zinc su...

2012-08-01T05:18:25Z

New page: '''Unreleased structure''' The entry 4b3e is ON HOLD until Paper Publication Authors: Strange, R.W., Hough, M.A., Antonyuk, S.V., Hasnain, S.S. Description: Structure of copper-zinc su...

New page

'''Unreleased structure'''

The entry 4b3e is ON HOLD until Paper Publication

Authors: Strange, R.W., Hough, M.A., Antonyuk, S.V., Hasnain, S.S.

Description: Structure of copper-zinc superoxide dismutase complexed with bicarbonate.