3m5d - Revision history

OCA at 08:48, 6 September 2023

2023-09-06T08:48:36Z

←Older revision		Revision as of 08:48, 6 September 2023
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	<StructureSection load='3m5d' size='340' side='right'caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3m5d' size='340' side='right'caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Xance Xance~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M5D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M5D FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PA9:N~2~~~-~~ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</scene>~~, ~~<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]] 2.2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3m4j\|3m4j]], [[3m4n\|3m4n]], [[3m5c\|3m5c]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>argF, argF', XCC2249 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~340 XANCE])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[https://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </~~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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [https://pdbe.org/3m5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [https://www.ebi.ac.uk/pdbsum/3m5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5d 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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [https://pdbe.org/3m5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [https://www.ebi.ac.uk/pdbsum/3m5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP]] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.	+	[https://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~N-acetylornithine carbamoyltransferase]]~~	+	[[Category: Xanthomonas campestris pv. campestris]]
-	~~[[Category: Xance~~]]	+	[[Category: Allewell NM]]
-	[[Category: Allewell~~, N M~~]]	+	[[Category: Li Y]]
-	[[Category: Li, Y]]	+	[[Category: Shi D]]
-	[[Category: Shi, D]]	+	[[Category: Tuchman M]]
-	[[Category: Tuchman, M]]	+	[[Category: Yu X]]
-	[[Category: Yu, X]]	+
-	~~[[Category: Transcarbamylase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:37, 6 October 2021

2021-10-06T05:37:18Z

←Older revision		Revision as of 05:37, 6 October 2021
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	==Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO==		==Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO==
-	<StructureSection load='3m5d' size='340' side='right' caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='3m5d' size='340' side='right'caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3M5D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M5D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</scene>, <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=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</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">[[3m4j\|3m4j]], [[3m4n\|3m4n]], [[3m5c\|3m5c]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m4j\|3m4j]], [[3m4n\|3m4n]], [[3m5c\|3m5c]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">argF, argF', XCC2249 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">argF, argF', XCC2249 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [~~http~~://pdbe.org/3m5d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3m5d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5d 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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [https://pdbe.org/3m5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [https://www.ebi.ac.uk/pdbsum/3m5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP]] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.	+	[[https://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP]] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m5d_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m5d_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 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 3m5d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3m5d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[N-acetylornithine carbamoyltransferase\|N-acetylornithine carbamoyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: N-acetylornithine carbamoyltransferase]]		[[Category: N-acetylornithine carbamoyltransferase]]
	[[Category: Xance]]		[[Category: Xance]]

OCA at 15:50, 5 August 2016

2016-08-05T15:50:40Z

←Older revision		Revision as of 15:50, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO==		==Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO==
	<StructureSection load='3m5d' size='340' side='right' caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3m5d' size='340' side='right' caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M5D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M5D FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</scene>, <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=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</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">[[3m4j\|3m4j]], [[3m4n\|3m4n]], [[3m5c\|3m5c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m4j\|3m4j]], [[3m4n\|3m4n]], [[3m5c\|3m5c]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">argF, argF', XCC2249 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 ~~Xanthomonas campestris pv. campestris~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">argF, argF', XCC2249 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 XANCE])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [http://www.ebi.ac.uk/pdbsum/3m5d 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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [http://pdbe.org/3m5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [http://www.ebi.ac.uk/pdbsum/3m5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m5d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3m5d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3m5d" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: N-acetylornithine carbamoyltransferase]]		[[Category: N-acetylornithine carbamoyltransferase]]
-	[[Category: ~~Xanthomonas campestris pv. campestris~~]]	+	[[Category: Xance]]
	[[Category: Allewell, N M]]		[[Category: Allewell, N M]]
	[[Category: Li, Y]]		[[Category: Li, Y]]

OCA at 03:44, 25 December 2014

2014-12-25T03:44:21Z

←Older revision		Revision as of 03:44, 25 December 2014
Line 9:		Line 9:
	<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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [http://www.ebi.ac.uk/pdbsum/3m5d 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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [http://www.ebi.ac.uk/pdbsum/3m5d PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AOTC_XANCP AOTC_XANCP]] Catalyzes the conversion of N-acetylornithine to N-acetylcitrulline in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:41, 18 December 2014

2014-12-18T16:41:38Z

←Older revision		Revision as of 16:41, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3m5d\| PDB=3m5d \| SCENE= }}~~	+	==Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO==
-	===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO===	+	<StructureSection load='3m5d' size='340' side='right' caption='[[3m5d]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20695527}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3m5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M5D FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PA9:N~2~-ACETYL-N~5~-(PHOSPHONOACETYL)-L-ORNITHINE'>PA9</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">[[3m4j\|3m4j]], [[3m4n\|3m4n]], [[3m5c\|3m5c]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">argF, argF', XCC2249 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=340 Xanthomonas campestris pv. campestris])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylornithine_carbamoyltransferase N-acetylornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.9 2.1.3.9] </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=3m5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m5d RCSB], [http://www.ebi.ac.uk/pdbsum/3m5d PDBsum]</span></td></tr>
		+	</table>
		+	== 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/m5/3m5d_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 ==
		+	N-Acetyl-l-ornithine transcarbamylase (AOTCase), rather than ornithine transcarbamylase (OTCase), is the essential carbamylase enzyme in the arginine biosynthesis of several plant and human pathogens. The specificity of this unique enzyme provides a potential target for controlling the spread of these pathogens. Recently, several crystal structures of AOTCase from Xanthomonas campestris (xc) have been determined. In these structures, an unexplained electron density at the tip of the Lys302 side chain was observed. Using (13)C NMR spectroscopy, we show herein that Lys302 is post-translationally carboxylated. The structure of wild-type AOTCase in a complex with the bisubstrate analogue N(delta)-(phosphonoacetyl)-N(alpha)-acetyl-l-ornithine (PALAO) indicates that the carboxyl group on Lys302 forms a strong hydrogen bonding network with surrounding active site residues, Lys252, Ser253, His293, and Glu92 from the adjacent subunit either directly or via a water molecule. Furthermore, the carboxyl group is involved in binding N-acetyl-l-ornithine via a water molecule. Activity assays with the wild-type enzyme and several mutants demonstrate that the post-translational modification of lysine 302 has an important role in catalysis.

-	~~==About this Structure==~~	+	Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.,Li Y, Yu X, Ho J, Fushman D, Allewell NM, Tuchman M, Shi D Biochemistry. 2010 Aug 17;49(32):6887-95. PMID:20695527<ref>PMID:20695527</ref>
-	~~[[3m5d]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Xanthomonas_campestris_pv~~.~~_campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:020695527</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: N-acetylornithine carbamoyltransferase]]		[[Category: N-acetylornithine carbamoyltransferase]]
	[[Category: Xanthomonas campestris pv. campestris]]		[[Category: Xanthomonas campestris pv. campestris]]
-	[[Category: Allewell, N M.]]	+	[[Category: Allewell, N M]]
-	[[Category: Li, Y.]]	+	[[Category: Li, Y]]
-	[[Category: Shi, D.]]	+	[[Category: Shi, D]]
-	[[Category: Tuchman, M.]]	+	[[Category: Tuchman, M]]
-	[[Category: Yu, X.]]	+	[[Category: Yu, X]]
	[[Category: Transcarbamylase]]		[[Category: Transcarbamylase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 23:13, 10 April 2013

2013-04-10T23:13:27Z

←Older revision		Revision as of 23:13, 10 April 2013
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-	[[Image:3m5d.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3m5d", 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_3m5d\| PDB=3m5d \| SCENE= }}		{{STRUCTURE_3m5d\| PDB=3m5d \| SCENE= }}
-
	===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO===		===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO===
-
-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20695527}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20695527 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20695527}}		{{ABSTRACT_PUBMED_20695527}}

Line 22:		Line 7:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20695527~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020695527</ref><references group="xtra"/><references/>
	[[Category: N-acetylornithine carbamoyltransferase]]		[[Category: N-acetylornithine carbamoyltransferase]]
	[[Category: Xanthomonas campestris pv. campestris]]		[[Category: Xanthomonas campestris pv. campestris]]
Line 30:		Line 15:
	[[Category: Tuchman, M.]]		[[Category: Tuchman, M.]]
	[[Category: Yu, X.]]		[[Category: Yu, X.]]
		+	[[Category: Transcarbamylase]]
		+	[[Category: Transferase]]

OCA: Protected "3m5d" [edit=sysop:move=sysop]

2011-01-12T05:25:24Z

Protected "3m5d" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:25, 12 January 2011

OCA at 05:25, 12 January 2011

2011-01-12T05:25:23Z

←Older revision		Revision as of 05:25, 12 January 2011
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3m5d.png\|left\|200px]]
-	[[Image:3m5d.~~jpg~~\|left\|200px]]	+

	<!--		<!--
Line 12:		Line 11:
	===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO===		===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20695527}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20695527 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20695527}}

	==About this Structure==		==About this Structure==
-	~~3M5D~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA].	+	[[3m5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20695527</ref><references group="xtra"/>
	[[Category: N-acetylornithine carbamoyltransferase]]		[[Category: N-acetylornithine carbamoyltransferase]]
	[[Category: Xanthomonas campestris pv. campestris]]		[[Category: Xanthomonas campestris pv. campestris]]
Line 22:		Line 30:
	[[Category: Tuchman, M.]]		[[Category: Tuchman, M.]]
	[[Category: Yu, X.]]		[[Category: Yu, X.]]
-	[[Category: Transcarbamylase]]
-	[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:38:14 2010''

OCA at 08:31, 28 July 2010

2010-07-28T08:31:32Z

←Older revision		Revision as of 08:31, 28 July 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3m5d.jpg\|left\|200px]]

-	The ~~entry 3m5d~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3m5d", 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_3m5d\| PDB=3m5d \| SCENE= }}

-	~~Authors: Li, Y., Yu, X., Allewell,~~ N~~.M., Tuchman, M., Shi, D.~~	+	===Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO===

-	Description: Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jun 2 08~~:27:37 2010''	+	==About this Structure==
		+	3M5D is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M5D OCA].
		+	[[Category: N-acetylornithine carbamoyltransferase]]
		+	[[Category: Xanthomonas campestris pv. campestris]]
		+	[[Category: Allewell, N M.]]
		+	[[Category: Li, Y.]]
		+	[[Category: Shi, D.]]
		+	[[Category: Tuchman, M.]]
		+	[[Category: Yu, X.]]
		+	[[Category: Transcarbamylase]]
		+	[[Category: Transferase]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:38:14 2010''

OCA at 04:23, 2 June 2010

2010-06-02T04:23:10Z

←Older revision		Revision as of 04:23, 2 June 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3m5d is ON HOLD	+	The entry 3m5d is ON HOLD until Paper Publication

	Authors: Li, Y., Yu, X., Allewell, N.M., Tuchman, M., Shi, D.		Authors: Li, Y., Yu, X., Allewell, N.M., Tuchman, M., Shi, D.
Line 7:		Line 7:
	Description: Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO		Description: Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar 24~~ 08:38:34 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 2 08:27:37 2010''