3e6v - Revision history

OCA at 12:58, 30 August 2023

2023-08-30T12:58:56Z

←Older revision		Revision as of 12:58, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='3e6v' size='340' side='right'caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>		<StructureSection load='3e6v' size='340' side='right'caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6V FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ABH:2(S)~~-~~AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>~~, ~~<scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.72Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[2aeb\|2aeb]], [[3e6k\|3e6k]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ARG1 ([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/Arginase Arginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1]~~ </~~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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [https://pdbe.org/3e6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [https://www.ebi.ac.uk/pdbsum/3e6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6v 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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [https://pdbe.org/3e6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [https://www.ebi.ac.uk/pdbsum/3e6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[https://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>	+	[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[https://omim.org/entry/207800 207800]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arginase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Christianson~~, D W~~]]	+	[[Category: Christianson DW]]
-	[[Category: Costanzo, L ~~Di]]~~	+	[[Category: Di Costanzo L]]
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Amino acid recognition]]~~	+
-	~~[[Category: Amino group recognition]]~~	+
-	~~[[Category: Arginine metabolism]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Manganese]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Mutant]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Urea cycle~~]]	+

OCA at 19:36, 20 October 2021

2021-10-20T19:36:31Z

←Older revision		Revision as of 19:36, 20 October 2021
Line 1:		Line 1:

	==X-ray structure of human arginase I-D183N mutant: the complex with ABH==		==X-ray structure of human arginase I-D183N mutant: the complex with ABH==
-	<StructureSection load='3e6v' size='340' side='right' caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>	+	<StructureSection load='3e6v' size='340' side='right'caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3E6V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6V FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3e6k\|3e6k]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2aeb\|2aeb]], [[3e6k\|3e6k]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([~~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">ARG1 ([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/Arginase Arginase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arginase Arginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [~~http~~://pdbe.org/3e6v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3e6v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6v 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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [https://pdbe.org/3e6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [https://www.ebi.ac.uk/pdbsum/3e6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[~~http~~://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>	+	[[https://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[https://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Arginase\|Arginase]]	+	*[[Arginase 3D structures\|Arginase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]
	[[Category: Costanzo, L Di]]		[[Category: Costanzo, L Di]]

OCA at 21:29, 2 December 2018

2018-12-02T21:29:55Z

←Older revision		Revision as of 21:29, 2 December 2018
Line 1:		Line 1:
		+
	==X-ray structure of human arginase I-D183N mutant: the complex with ABH==		==X-ray structure of human arginase I-D183N mutant: the complex with ABH==
	<StructureSection load='3e6v' size='340' side='right' caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>		<StructureSection load='3e6v' size='340' side='right' caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([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">ARG1 ([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/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [http://pdbe.org/3e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [http://www.ebi.ac.uk/pdbsum/3e6v 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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [http://pdbe.org/3e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [http://www.ebi.ac.uk/pdbsum/3e6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/3e6v_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/3e6v_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 41:		Line 42:
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]
	[[Category: Costanzo, L Di]]		[[Category: Costanzo, L Di]]
		+	[[Category: Alternative splicing]]
	[[Category: Amino acid recognition]]		[[Category: Amino acid recognition]]
	[[Category: Amino group recognition]]		[[Category: Amino group recognition]]
	[[Category: Arginine metabolism]]		[[Category: Arginine metabolism]]
		+	[[Category: Cytoplasm]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
Line 50:		Line 53:
	[[Category: Mutant]]		[[Category: Mutant]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
		+	[[Category: Polymorphism]]
	[[Category: Urea cycle]]		[[Category: Urea cycle]]

OCA at 01:04, 10 February 2016

2016-02-10T01:04:22Z

←Older revision		Revision as of 01:04, 10 February 2016
Line 2:		Line 2:
	<StructureSection load='3e6v' size='340' side='right' caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>		<StructureSection load='3e6v' size='340' side='right' caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E6V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E6V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3e6k\|3e6k]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3e6k\|3e6k]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([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">ARG1 ([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/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [http://www.ebi.ac.uk/pdbsum/3e6v 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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [http://pdbe.org/3e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [http://www.ebi.ac.uk/pdbsum/3e6v PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 19:
	<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=3e6v ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	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 3e6v" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Arginase]]		[[Category: Arginase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]
	[[Category: Costanzo, L Di]]		[[Category: Costanzo, L Di]]

OCA at 10:42, 25 December 2014

2014-12-25T10:42:45Z

←Older revision		Revision as of 10:42, 25 December 2014
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	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>		[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
-	== Function ==
-
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:25, 18 December 2014

2014-12-18T13:25:18Z

←Older revision		Revision as of 13:25, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3e6v\| PDB=3e6v \| SCENE= }}~~	+	==X-ray structure of human arginase I-D183N mutant: the complex with ABH==
-	===X-ray structure of human arginase I-D183N mutant: the complex with ABH===	+	<StructureSection load='3e6v' size='340' side='right' caption='[[3e6v]], [[Resolution\|resolution]] 1.72Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19093830}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3e6v]] 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=3E6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E6V FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABH:2(S)-AMINO-6-BORONOHEXANOIC+ACID'>ABH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2aeb\|2aeb]], [[3e6k\|3e6k]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARG1 ([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/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=3e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e6v RCSB], [http://www.ebi.ac.uk/pdbsum/3e6v PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref> <ref>PMID:7649538</ref>
		+	== Function ==

-	==~~Disease~~==	+	== Evolutionary Conservation ==
-	[[~~http~~://~~www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~ARGI1_HUMAN ARGI1_HUMAN~~]~~] Defects in ARG1 are~~ the ~~cause of argininemia (ARGIN)~~ [~~MIM:~~[http://~~omim~~.~~org~~/~~entry~~/~~207800 207800~~]~~]; also known as hyperargininemia~~. ~~Argininemia~~ is a ~~rare autosomal recessive disorder~~ of the ~~urea cycle~~. ~~Arginine is elevated~~ in the ~~blood~~ and ~~cerebrospinal fluid~~, and ~~periodic hyperammonemia occurs~~. ~~Clinical manifestations include developmental delay~~, ~~seizures~~, ~~mental retardation~~, ~~hypotonia~~, ~~ataxia, progressive spastic quadriplegia~~.~~<ref>PMID:1463019</ref><ref>PMID:7649538</ref>~~	+	[[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/e6/3e6v_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 ==
		+	Arginase is a binuclear manganese metalloenzyme that serves as a therapeutic target for the treatment of asthma, erectile dysfunction, and atherosclerosis. In order to better understand the molecular basis of inhibitor affinity, we have employed site-directed mutagenesis, enzyme kinetics, and X-ray crystallography to probe the molecular recognition of the amino acid moiety (i.e., the alpha-amino and alpha-carboxylate groups) of substrate l-arginine and inhibitors in the active site of arginase I. Specifically, we focus on (1) a water-mediated hydrogen bond between the substrate alpha-carboxylate and T135, (2) a direct hydrogen bond between the substrate alpha-carboxylate and N130, and (3) a direct charged hydrogen bond between the substrate alpha-amino group and D183. Amino acid substitutions for T135, N130, and D183 generally compromise substrate affinity as reflected by increased K(M) values but have less pronounced effects on catalytic function as reflected by minimal variations of k(cat). As with substrate K(M) values, inhibitor K(d) values increase for binding to enzyme mutants and suggest that the relative contribution of intermolecular interactions to amino acid affinity in the arginase active site is water-mediated hydrogen bond < direct hydrogen bond < direct charged hydrogen bond. Structural comparisons of arginase with the related binuclear manganese metalloenzymes agmatinase and proclavaminic acid amidinohydrolase suggest that the evolution of substrate recognition in the arginase fold occurs by mutation of residues contained in specificity loops flanking the mouth of the active site (especially loops 4 and 5), thereby allowing diverse guanidinium substrates to be accommodated for catalysis.

-	~~==About this Structure==~~	+	Probing the specificity determinants of amino acid recognition by arginase.,Shishova EY, Di Costanzo L, Emig FA, Ash DE, Christianson DW Biochemistry. 2009 Jan 13;48(1):121-31. PMID:19093830<ref>PMID:19093830</ref>
-	~~[[3e6v]] 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=3E6V OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group~~=~~"xtra">PMID:019093830</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+
		+	==See Also==
		+	*[[Arginase\|Arginase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Christianson, D W.]]	+	[[Category: Christianson, D W]]
-	[[Category: Costanzo, L Di.]]	+	[[Category: Costanzo, L Di]]
	[[Category: Amino acid recognition]]		[[Category: Amino acid recognition]]
	[[Category: Amino group recognition]]		[[Category: Amino group recognition]]

OCA at 21:45, 24 March 2013

2013-03-24T21:45:02Z

←Older revision		Revision as of 21:45, 24 March 2013
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-	[[Image:3e6v.png\|left\|200px]]
-
	{{STRUCTURE_3e6v\| PDB=3e6v \| SCENE= }}		{{STRUCTURE_3e6v\| PDB=3e6v \| SCENE= }}
-
	===X-ray structure of human arginase I-D183N mutant: the complex with ABH===		===X-ray structure of human arginase I-D183N mutant: the complex with ABH===
		+	{{ABSTRACT_PUBMED_19093830}}

-	~~{{ABSTRACT_PUBMED_19093830}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref><ref>PMID:7649538</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019093830</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019093830</ref><references group="xtra"/><references/>
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "3e6v" [edit=sysop:move=sysop]

2013-01-09T08:47:51Z

Protected "3e6v" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:47, 9 January 2013

OCA at 08:47, 9 January 2013

2013-01-09T08:47:48Z

←Older revision		Revision as of 08:47, 9 January 2013
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-	{{Seed}}
	[[Image:3e6v.png\|left\|200px]]		[[Image:3e6v.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3e6v", 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),
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-	-->
	{{STRUCTURE_3e6v\| PDB=3e6v \| SCENE= }}		{{STRUCTURE_3e6v\| PDB=3e6v \| SCENE= }}

	===X-ray structure of human arginase I-D183N mutant: the complex with ABH===		===X-ray structure of human arginase I-D183N mutant: the complex with ABH===

-
-	<!--
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-	(as it appears on PubMed at http://www.pubmed.gov), where 19093830 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19093830}}		{{ABSTRACT_PUBMED_19093830}}

	==About this Structure==		==About this Structure==
-	~~3E6V~~ is a 2 ~~chains~~ structure with ~~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=3E6V OCA].	+	[[3e6v]] 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=3E6V OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19093830~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019093830</ref><references group="xtra"/>
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Christianson, D W.]]		[[Category: Christianson, D W.]]
	[[Category: Costanzo, L Di.]]		[[Category: Costanzo, L Di.]]
-	[[Category: Alternative splicing]]
	[[Category: Amino acid recognition]]		[[Category: Amino acid recognition]]
	[[Category: Amino group recognition]]		[[Category: Amino group recognition]]
	[[Category: Arginine metabolism]]		[[Category: Arginine metabolism]]
-	[[Category: Cytoplasm]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
Line 39:		Line 25:
	[[Category: Mutant]]		[[Category: Mutant]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
	[[Category: Urea cycle]]		[[Category: Urea cycle]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 11:29:17 2010''

OCA at 08:20, 22 September 2010

2010-09-22T08:20:19Z

←Older revision		Revision as of 08:20, 22 September 2010
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	==About this Structure==		==About this Structure==
-	3E6V is a ~~[[Single protein]]~~ structure ~~of 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=3E6V OCA].	+	3E6V is a 2 chains structure with 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=3E6V OCA].

	==Reference==		==Reference==
-	~~Probing the specificity determinants of amino acid recognition by arginase., Shishova EY, Di Costanzo L, Emig FA, Ash DE, Christianson DW, Biochemistry. 2009 Jan 13;48(1):121-31.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/19093830 19093830]~~	+	<ref group="xtra">PMID:19093830</ref><references group="xtra"/>
	[[Category: Arginase]]		[[Category: Arginase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: ~~Single protein~~]]	+	[[Category: Christianson, D W.]]
-	[[Category: ~~Pdbx_ordinal=~~, ~~<PDBx:audit_author~~.]]	+	[[Category: Costanzo, L Di.]]
	[[Category: Alternative splicing]]		[[Category: Alternative splicing]]
	[[Category: Amino acid recognition]]		[[Category: Amino acid recognition]]
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	[[Category: Urea cycle]]		[[Category: Urea cycle]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar~~ 11 20:12:~~11 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 11:29:17 2010''