4gyr - Revision history

OCA at 15:59, 14 March 2024

OCA — Thu, 14 Mar 2024 15:59:57 GMT

←Older revision		Revision as of 15:59, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Granulibacter_bethesdensis_CGDNIH1 Granulibacter bethesdensis CGDNIH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GYR FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Granulibacter_bethesdensis_CGDNIH1 Granulibacter bethesdensis CGDNIH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GYR FirstGlance]. <br>
-	</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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [https://pdbe.org/4gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [https://www.ebi.ac.uk/pdbsum/4gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyr ProSAT]</span></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]] 2.8Å</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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [https://pdbe.org/4gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [https://www.ebi.ac.uk/pdbsum/4gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q0BRB0_GRABC Q0BRB0_GRABC]		[https://www.uniprot.org/uniprot/Q0BRB0_GRABC Q0BRB0_GRABC]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Allophanate hydrolase (AH) catalyzes the hydrolysis of allophanate, an intermediate in atrazine degradation and urea catabolism pathways, to NH(3) and CO(2). AH belongs to the amidase signature family, which is characterized by a conserved block of 130 amino acids rich in Gly and Ser and a Ser-cis-Ser-Lys catalytic triad. In this study, the first structures of AH from Granulibacter bethesdensis were determined, with and without the substrate analogue malonate, to 2.2 and 2.8 A, respectively. The structures confirm the identity of the catalytic triad residues and reveal an altered dimerization interface that is not conserved in the amidase signature family. The structures also provide insights into previously unrecognized substrate specificity determinants in AH. Two residues, Tyr(299) and Arg(307), are within hydrogen bonding distance of a carboxylate moiety of malonate. Both Tyr(299) and Arg(307) were mutated, and the resulting modified enzymes revealed >3 order of magnitude reductions in both catalytic efficiency and substrate stringency. It is proposed that Tyr(299) and Arg(307) serve to anchor and orient the substrate for attack by the catalytic nucleophile, Ser(172). The structure further suggests the presence of a unique C-terminal domain in AH. While this domain is conserved, it does not contribute to catalysis or to the structural integrity of the core domain, suggesting that it may play a role in mediating transient and specific interactions with the urea carboxylase component of urea amidolyase. Analysis of the AH active site architecture offers new insights into common determinants of catalysis and specificity among divergent members of the amidase signature family.
-
-	The Structure of Allophanate Hydrolase from Granulibacter bethesdensis Provides Insights into Substrate Specificity in the Amidase Signature Family.,Lin Y, St Maurice M Biochemistry. 2013 Jan 29;52(4):690-700. doi: 10.1021/bi301242m. Epub 2013 Jan, 18. PMID:23282241<ref>PMID:23282241</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gyr" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:27, 26 October 2022

OCA — Wed, 26 Oct 2022 07:27:25 GMT

←Older revision		Revision as of 07:27, 26 October 2022
Line 1:		Line 1:

	==Granulibacter bethesdensis allophanate hydrolase apo==		==Granulibacter bethesdensis allophanate hydrolase apo==
-	<StructureSection load='4gyr' size='340' side='right' caption='[[4gyr]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='4gyr' size='340' side='right'caption='[[4gyr]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Grabc Grabc~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GYR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Granulibacter_bethesdensis_CGDNIH1 Granulibacter bethesdensis CGDNIH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GYR FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gys\|4gys]]</td></tr>~~	+	</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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [https://pdbe.org/4gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [https://www.ebi.ac.uk/pdbsum/4gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyr ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GbCGDNIH1_1744 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391165 GRABC])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allophanate_hydrolase Allophanate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.54 3.5.1.54] </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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [~~http~~://pdbe.org/4gyr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gyr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyr ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q0BRB0_GRABC Q0BRB0_GRABC]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Allophanate hydrolase~~]]	+	[[Category: Granulibacter bethesdensis CGDNIH1]]
-	[[Category: ~~Grabc~~]]	+	[[Category: Large Structures]]
-	[[Category: Lin, Y]]	+	[[Category: Lin Y]]
-	[[Category: Maurice, M ~~St]]~~	+	[[Category: St Maurice M]]
-	~~[[Category: Amidase signature family enzyme]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 19:59, 15 December 2016

OCA — Thu, 15 Dec 2016 19:59:15 GMT

←Older revision		Revision as of 19:59, 15 December 2016
Line 1:		Line 1:
		+
	==Granulibacter bethesdensis allophanate hydrolase apo==		==Granulibacter bethesdensis allophanate hydrolase apo==
	<StructureSection load='4gyr' size='340' side='right' caption='[[4gyr]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4gyr' size='340' side='right' caption='[[4gyr]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Granulibacter_bethesdensis_cgdnih1 Granulibacter bethesdensis cgdnih1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GYR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Grabc Grabc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GYR FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gys\|4gys]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gys\|4gys]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GbCGDNIH1_1744 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391165 ~~Granulibacter bethesdensis CGDNIH1~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GbCGDNIH1_1744 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391165 GRABC])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allophanate_hydrolase Allophanate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.54 3.5.1.54] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allophanate_hydrolase Allophanate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.54 3.5.1.54] </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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [http://www.ebi.ac.uk/pdbsum/4gyr 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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [http://pdbe.org/4gyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [http://www.ebi.ac.uk/pdbsum/4gyr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyr ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 4gyr" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Allophanate hydrolase]]		[[Category: Allophanate hydrolase]]
-	[[Category: ~~Granulibacter bethesdensis cgdnih1~~]]	+	[[Category: Grabc]]
	[[Category: Lin, Y]]		[[Category: Lin, Y]]
	[[Category: Maurice, M St]]		[[Category: Maurice, M St]]
	[[Category: Amidase signature family enzyme]]		[[Category: Amidase signature family enzyme]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 09:33, 10 December 2014

OCA — Wed, 10 Dec 2014 09:33:55 GMT

←Older revision		Revision as of 09:33, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4gyr.~~png~~\|~~left~~\|~~200px~~]]	+	==Granulibacter bethesdensis allophanate hydrolase apo==
		+	<StructureSection load='4gyr' size='340' side='right' caption='[[4gyr]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gyr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Granulibacter_bethesdensis_cgdnih1 Granulibacter bethesdensis cgdnih1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GYR FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gys\|4gys]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GbCGDNIH1_1744 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391165 Granulibacter bethesdensis CGDNIH1])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allophanate_hydrolase Allophanate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.54 3.5.1.54] </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=4gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gyr RCSB], [http://www.ebi.ac.uk/pdbsum/4gyr PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Allophanate hydrolase (AH) catalyzes the hydrolysis of allophanate, an intermediate in atrazine degradation and urea catabolism pathways, to NH(3) and CO(2). AH belongs to the amidase signature family, which is characterized by a conserved block of 130 amino acids rich in Gly and Ser and a Ser-cis-Ser-Lys catalytic triad. In this study, the first structures of AH from Granulibacter bethesdensis were determined, with and without the substrate analogue malonate, to 2.2 and 2.8 A, respectively. The structures confirm the identity of the catalytic triad residues and reveal an altered dimerization interface that is not conserved in the amidase signature family. The structures also provide insights into previously unrecognized substrate specificity determinants in AH. Two residues, Tyr(299) and Arg(307), are within hydrogen bonding distance of a carboxylate moiety of malonate. Both Tyr(299) and Arg(307) were mutated, and the resulting modified enzymes revealed >3 order of magnitude reductions in both catalytic efficiency and substrate stringency. It is proposed that Tyr(299) and Arg(307) serve to anchor and orient the substrate for attack by the catalytic nucleophile, Ser(172). The structure further suggests the presence of a unique C-terminal domain in AH. While this domain is conserved, it does not contribute to catalysis or to the structural integrity of the core domain, suggesting that it may play a role in mediating transient and specific interactions with the urea carboxylase component of urea amidolyase. Analysis of the AH active site architecture offers new insights into common determinants of catalysis and specificity among divergent members of the amidase signature family.

-	~~{{STRUCTURE_4gyr\| PDB=4gyr \| SCENE= }}~~	+	The Structure of Allophanate Hydrolase from Granulibacter bethesdensis Provides Insights into Substrate Specificity in the Amidase Signature Family.,Lin Y, St Maurice M Biochemistry. 2013 Jan 29;52(4):690-700. doi: 10.1021/bi301242m. Epub 2013 Jan, 18. PMID:23282241<ref>PMID:23282241</ref>

-	~~===Granulibacter bethesdensis allophanate hydrolase apo===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23282241}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4gyr]] is a 2 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Granulibacter_bethesdensis_cgdnih1 Granulibacter bethesdensis cgdnih1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA].	+	</StructureSection>
	[[Category: Allophanate hydrolase]]		[[Category: Allophanate hydrolase]]
	[[Category: Granulibacter bethesdensis cgdnih1]]		[[Category: Granulibacter bethesdensis cgdnih1]]
-	[[Category: Lin, Y.]]	+	[[Category: Lin, Y]]
-	[[Category: Maurice, M St.]]	+	[[Category: Maurice, M St]]
	[[Category: Amidase signature family enzyme]]		[[Category: Amidase signature family enzyme]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 12:36, 20 February 2013

OCA — Wed, 20 Feb 2013 12:36:39 GMT

←Older revision		Revision as of 12:36, 20 February 2013
Line 1:		Line 1:
-	[[Image:4gyr.~~jpg~~\|left\|200px]]	+	[[Image:4gyr.png\|left\|200px]]

	{{STRUCTURE_4gyr\| PDB=4gyr \| SCENE= }}		{{STRUCTURE_4gyr\| PDB=4gyr \| SCENE= }}
Line 12:		Line 12:
	[[Category: Granulibacter bethesdensis cgdnih1]]		[[Category: Granulibacter bethesdensis cgdnih1]]
	[[Category: Lin, Y.]]		[[Category: Lin, Y.]]
-	[[Category: Maurice, M St..]]	+	[[Category: Maurice, M St.]]
	[[Category: Amidase signature family enzyme]]		[[Category: Amidase signature family enzyme]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 12:22, 30 January 2013

OCA — Wed, 30 Jan 2013 12:22:32 GMT

←Older revision		Revision as of 12:22, 30 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gyr.jpg\|left\|200px]]

-	~~The entry~~ 4gyr ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gyr\| PDB=4gyr \| SCENE= }}

-	~~Authors: Lin, Y., St. Maurice, M.~~	+	===Granulibacter bethesdensis allophanate hydrolase apo===

-	~~Description~~: Granulibacter bethesdensis ~~allophanate~~ hydrolase ~~apo~~	+	{{ABSTRACT_PUBMED_23282241}}
		+
		+	==About this Structure==
		+	[[4gyr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Granulibacter_bethesdensis_cgdnih1 Granulibacter bethesdensis cgdnih1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYR OCA].
		+	[[Category: Allophanate hydrolase]]
		+	[[Category: Granulibacter bethesdensis cgdnih1]]
		+	[[Category: Lin, Y.]]
		+	[[Category: Maurice, M St..]]
		+	[[Category: Amidase signature family enzyme]]
		+	[[Category: Hydrolase]]

OCA at 10:57, 19 December 2012

OCA — Wed, 19 Dec 2012 10:57:38 GMT

←Older revision		Revision as of 10:57, 19 December 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gyr is ON HOLD	+	The entry 4gyr is ON HOLD until Paper Publication

	Authors: Lin, Y., St. Maurice, M.		Authors: Lin, Y., St. Maurice, M.

	Description: Granulibacter bethesdensis allophanate hydrolase apo		Description: Granulibacter bethesdensis allophanate hydrolase apo

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

OCA — Wed, 12 Sep 2012 04:56:56 GMT

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

←Older revision

Revision as of 04:56, 12 September 2012

OCA: New page: '''Unreleased structure''' The entry 4gyr is ON HOLD Authors: Lin, Y., St. Maurice, M. Description: Granulibacter bethesdensis allophanate hydrolase apo

OCA — Wed, 12 Sep 2012 04:56:55 GMT

New page: '''Unreleased structure''' The entry 4gyr is ON HOLD Authors: Lin, Y., St. Maurice, M. Description: Granulibacter bethesdensis allophanate hydrolase apo

New page

'''Unreleased structure'''

The entry 4gyr is ON HOLD

Authors: Lin, Y., St. Maurice, M.

Description: Granulibacter bethesdensis allophanate hydrolase apo