3a6f - Revision history

OCA at 14:13, 1 November 2023

OCA — Wed, 01 Nov 2023 14:13:39 GMT

←Older revision		Revision as of 14:13, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3a6f' size='340' side='right'caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='3a6f' size='340' side='right'caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A6F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A6F FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>~~, ~~<scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.78Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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/Creatininase Creatininase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10]~~ </~~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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [https://pdbe.org/3a6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [https://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f 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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [https://pdbe.org/3a6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [https://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU]] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>	+	[https://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus fluorescens putidus flugge 1886]]
-	[[Category: Creatininase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ito, K]]	+	[[Category: Pseudomonas putida]]
-	[[Category: Nakajima, Y]]	+	[[Category: Ito K]]
-	[[Category: Yamashita, K]]	+	[[Category: Nakajima Y]]
-	[[Category: Yoshimoto, T]]	+	[[Category: Yamashita K]]
-	~~[[Category: Creatinine amidohydrolase]]~~	+	[[Category: Yoshimoto T]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Urease-related amidohydrolase superfamily~~]]	+

OCA at 07:23, 10 November 2021

OCA — Wed, 10 Nov 2021 07:23:13 GMT

←Older revision		Revision as of 07:23, 10 November 2021
Line 3:		Line 3:
	<StructureSection load='3a6f' size='340' side='right'caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='3a6f' size='340' side='right'caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3A6F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A6F FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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">[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [~~http~~://pdbe.org/3a6f PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f 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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [https://pdbe.org/3a6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [https://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU]] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>	+	[[https://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU]] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:17, 29 July 2020

OCA — Wed, 29 Jul 2020 12:17:54 GMT

←Older revision		Revision as of 12:17, 29 July 2020
Line 1:		Line 1:

	==W174F mutant creatininase, Type II==		==W174F mutant creatininase, Type II==
-	<StructureSection load='3a6f' size='340' side='right' caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>	+	<StructureSection load='3a6f' size='340' side='right'caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3A6F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A6F FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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">[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://pdbe.org/3a6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://pdbe.org/3a6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	[[Category: Bacillus fluorescens putidus flugge 1886]]		[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Creatininase]]		[[Category: Creatininase]]
		+	[[Category: Large Structures]]
	[[Category: Ito, K]]		[[Category: Ito, K]]
	[[Category: Nakajima, Y]]		[[Category: Nakajima, Y]]

OCA at 08:06, 24 October 2018

OCA — Wed, 24 Oct 2018 08:06:11 GMT

←Older revision		Revision as of 08:06, 24 October 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/3a6f_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/3a6f_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>

OCA at 17:53, 5 August 2016

OCA — Fri, 05 Aug 2016 17:53:32 GMT

←Older revision		Revision as of 17:53, 5 August 2016
Line 1:		Line 1:
		+
	==W174F mutant creatininase, Type II==		==W174F mutant creatininase, Type II==
	<StructureSection load='3a6f' size='340' side='right' caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>		<StructureSection load='3a6f' size='340' side='right' caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f 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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://pdbe.org/3a6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a6f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		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=3a6f ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		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 3a6f" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:46, 25 December 2014

OCA — Thu, 25 Dec 2014 20:46:57 GMT

←Older revision		Revision as of 20:46, 25 December 2014
Line 8:		Line 8:
	<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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f 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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU]] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Bacillus fluorescens putidus flugge 1886]]		[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Creatininase]]		[[Category: Creatininase]]
-	[[Category: Ito, K.]]	+	[[Category: Ito, K]]
-	[[Category: Nakajima, Y.]]	+	[[Category: Nakajima, Y]]
-	[[Category: Yamashita, K.]]	+	[[Category: Yamashita, K]]
-	[[Category: Yoshimoto, T.]]	+	[[Category: Yoshimoto, T]]
	[[Category: Creatinine amidohydrolase]]		[[Category: Creatinine amidohydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Urease-related amidohydrolase superfamily]]		[[Category: Urease-related amidohydrolase superfamily]]

OCA at 06:48, 10 October 2014

OCA — Fri, 10 Oct 2014 06:48:27 GMT

←Older revision		Revision as of 06:48, 10 October 2014
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-	~~{{STRUCTURE_3a6f\| PDB~~=3a6f \| ~~SCENE~~= }}	+	==W174F mutant creatininase, Type II==
-	===~~W174F mutant creatininase~~, ~~Type~~ II===	+	<StructureSection load='3a6f' size='340' side='right' caption='[[3a6f]], [[Resolution\|resolution]] 1.78Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20043918}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3a6f]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A6F FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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">[[1j2t\|1j2t]], [[1j2u\|1j2u]], [[1v7z\|1v7z]], [[3a6d\|3a6d]], [[3a6e\|3a6e]], [[3a6g\|3a6g]], [[3a6h\|3a6h]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Creatininase Creatininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.10 3.5.2.10] </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=3a6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a6f RCSB], [http://www.ebi.ac.uk/pdbsum/3a6f 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/a6/3a6f_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 ==
		+	Creatininase is a binuclear zinc enzyme and catalyzes the reversible conversion of creatinine to creatine. It exhibits an open-closed conformational change upon substrate binding, and the differences in the conformations of Tyr121, Trp154, and the loop region containing Trp174 were evident in the enzyme-creatine complex when compared to those in the ligand-free enzyme. We have determined the crystal structure of the enzyme complexed with a 1-methylguanidine. All subunits in the complex existed as the closed form, and the binding mode of creatinine was estimated. Site-directed mutagenesis revealed that the hydrophobic residues that show conformational change upon substrate binding are important for the enzyme activity. We propose a catalytic mechanism of creatininase in which two water molecules have significant roles. The first molecule is a hydroxide ion (Wat1) that is bound as a bridge between the two metal ions and attacks the carbonyl carbon of the substrate. The second molecule is a water molecule (Wat2) that is bound to the carboxyl group of Glu122 and functions as a proton donor in catalysis. The activity of the E122Q mutant was very low and it was only partially restored by the addition of ZnCl(2) or MnCl(2). In the E122Q mutant, k(cat) is drastically decreased, indicating that Glu122 is important for catalysis. X-ray crystallographic study and the atomic absorption spectrometry analysis of the E122Q mutant-substrate complex revealed that the drastic decrease of the activity of the E122Q was caused by not only the loss of one Zn ion at the Metal1 site but also a critical function of Glu122, which most likely exists for a proton transfer step through Wat2.

-	~~==Function==~~	+	Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase.,Yamashita K, Nakajima Y, Matsushita H, Nishiya Y, Yamazawa R, Wu YF, Matsubara F, Oyama H, Ito K, Yoshimoto T J Mol Biol. 2010 Mar 5;396(4):1081-96. Epub 2010 Jan 4. PMID:20043918<ref>PMID:20043918</ref>
-	~~[[http://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU]] Cyclic amidohydrolase that catalyzes~~ the ~~reversible conversion~~ of ~~creatinine to creatine~~. ~~Is also active toward glycocyamidine~~, ~~though the reaction rate is very low~~, ~~but it is completely inert toward hydantoin and its derivatives~~.<ref>PMID:~~500580~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3a6f]] is~~ a ~~6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020043918</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bacillus fluorescens putidus flugge 1886]]		[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Creatininase]]		[[Category: Creatininase]]

OCA at 06:11, 22 January 2014

OCA — Wed, 22 Jan 2014 06:11:00 GMT

←Older revision		Revision as of 06:11, 22 January 2014
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-	[[Image:3a6f.png\|left\|200px]]
-
	{{STRUCTURE_3a6f\| PDB=3a6f \| SCENE= }}		{{STRUCTURE_3a6f\| PDB=3a6f \| SCENE= }}
-
	===W174F mutant creatininase, Type II===		===W174F mutant creatininase, Type II===
		+	{{ABSTRACT_PUBMED_20043918}}

-	~~{{ABSTRACT_PUBMED_20043918}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU]] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>

	==About this Structure==		==About this Structure==
-	[[3a6f]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Pseudomonas_putida Pseudomonas putida~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA].	+	[[3a6f]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020043918</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020043918</ref><references group="xtra"/><references/>
		+	[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Creatininase]]		[[Category: Creatininase]]
-	[[Category: Pseudomonas putida]]
	[[Category: Ito, K.]]		[[Category: Ito, K.]]
	[[Category: Nakajima, Y.]]		[[Category: Nakajima, Y.]]

OCA: Protected "3a6f" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 20:24:03 GMT

Protected "3a6f" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:24, 7 January 2013

OCA at 20:23, 7 January 2013

OCA — Mon, 07 Jan 2013 20:23:59 GMT

←Older revision		Revision as of 20:23, 7 January 2013
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-	~~{{Seed}}~~	+	[[Image:3a6f.png\|left\|200px]]
-	[[Image:3a6f.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3a6f", 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_3a6f\| PDB=3a6f \| SCENE= }}		{{STRUCTURE_3a6f\| PDB=3a6f \| SCENE= }}

	===W174F mutant creatininase, Type II===		===W174F mutant creatininase, Type II===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20043918}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20043918 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20043918}}		{{ABSTRACT_PUBMED_20043918}}

	==About this Structure==		==About this Structure==
-	~~3A6F~~ is a 6 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA].	+	[[3a6f]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A6F OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20043918~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020043918</ref><references group="xtra"/>
	[[Category: Creatininase]]		[[Category: Creatininase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
Line 31:		Line 19:
	[[Category: Yoshimoto, T.]]		[[Category: Yoshimoto, T.]]
	[[Category: Creatinine amidohydrolase]]		[[Category: Creatinine amidohydrolase]]
		+	[[Category: Hydrolase]]
	[[Category: Urease-related amidohydrolase superfamily]]		[[Category: Urease-related amidohydrolase superfamily]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 17:11:23 2010''