5m66 - Revision history

OCA at 18:27, 1 November 2023

OCA — Wed, 01 Nov 2023 18:27:17 GMT

←Older revision		Revision as of 18:27, 1 November 2023
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	==Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine==		==Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine==
-	<StructureSection load='5m66' size='340' side='right' caption='[[5m66]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='5m66' size='340' side='right'caption='[[5m66]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5m66]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_49852 Atcc 49852~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M66 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5M66 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5m66]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_elkanii Bradyrhizobium elkanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M66 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=ADN:ADENOSINE'~~>~~ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE~~-~~ADENINE-DINUCLEOTIDE'>NAD</scene>~~, ~~<scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.951Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[4lvc\|4lvc]], [[3ond\|3ond]], [[3one\|3one]], [[3onf\|3onf]], [[1a7a\|1a7a]], [[1v8b\|1v8b]], [[3ce6\|3ce6]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~"><~~b>[[Gene\|Gene~~:~~]]</b~~></td><~~td class~~=~~"sblockDat">ahcY, BeSAHase ([http~~:~~//www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29448 ATCC 49852])</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=5m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m66 OCA], [https://pdbe.org/5m66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m66 RCSB], [https://www.ebi.ac.uk/pdbsum/5m66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m66 ProSAT]</span></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1]~~ </~~span~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m66 OCA], [~~http~~://pdbe.org/5m66 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5m66 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5m66 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5m66 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/SAHH_BRAEL SAHH_BRAEL]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Adenosylhomocysteinase~~]]	+	[[Category: Bradyrhizobium elkanii]]
-	[[Category: ~~Atcc 49852~~]]	+	[[Category: Large Structures]]
-	[[Category: Jaskolski, M]]	+	[[Category: Jaskolski M]]
-	[[Category: Manszewski, T]]	+	[[Category: Manszewski T]]
-	~~[[Category: Adenosine]]~~	+
-	~~[[Category: Conformational transition]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Molecular gate]]~~	+
-	~~[[Category: Nad]]~~	+
-	~~[[Category: Nitrogen fixation]]~~	+
-	~~[[Category: Sah]]~~	+
-	~~[[Category: Sahase]]~~	+
-	~~[[Category: Sam-dependent methylation]]~~	+
-	~~[[Category: Symbiotic bacteria~~]]	+

OCA at 22:02, 9 August 2018

OCA — Thu, 09 Aug 2018 22:02:25 GMT

←Older revision		Revision as of 22:02, 9 August 2018
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	<StructureSection load='5m66' size='340' side='right' caption='[[5m66]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='5m66' size='340' side='right' caption='[[5m66]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5m66]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M66 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5m66]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49852 Atcc 49852]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M66 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lvc\|4lvc]], [[3ond\|3ond]], [[3one\|3one]], [[3onf\|3onf]], [[1a7a\|1a7a]], [[1v8b\|1v8b]], [[3ce6\|3ce6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lvc\|4lvc]], [[3ond\|3ond]], [[3one\|3one]], [[3onf\|3onf]], [[1a7a\|1a7a]], [[1v8b\|1v8b]], [[3ce6\|3ce6]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ahcY, BeSAHase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29448 ATCC 49852])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m66 OCA], [http://pdbe.org/5m66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m66 RCSB], [http://www.ebi.ac.uk/pdbsum/5m66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m66 ProSAT]</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=5m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m66 OCA], [http://pdbe.org/5m66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m66 RCSB], [http://www.ebi.ac.uk/pdbsum/5m66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m66 ProSAT]</span></td></tr>
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	</div>		</div>
	<div class="pdbe-citations 5m66" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5m66" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[S-adenosylhomocysteine hydrolase\|S-adenosylhomocysteine hydrolase]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Adenosylhomocysteinase]]		[[Category: Adenosylhomocysteinase]]
		+	[[Category: Atcc 49852]]
	[[Category: Jaskolski, M]]		[[Category: Jaskolski, M]]
	[[Category: Manszewski, T]]		[[Category: Manszewski, T]]

OCA at 11:51, 3 August 2017

OCA — Thu, 03 Aug 2017 11:51:05 GMT

←Older revision		Revision as of 11:51, 3 August 2017
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	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	S-Adenosyl-L-homocysteine hydrolase (SAHase) ~~is involved in~~ the ~~enzymatic regulation of S-adenosyl-L-methionine~~ (~~SAM~~)-~~dependent methylation reactions. After methyl-group transfer from SAM~~, ~~S-adenosyl-L-homocysteine~~ (~~SAH~~) ~~is formed as a byproduct~~, ~~which in turn is hydrolyzed to adenosine~~ (~~Ado~~) and ~~homocysteine~~ (~~Hcy~~) ~~by SAHase~~. The crystal ~~structure~~ of ~~BeSAHase~~, ~~an SAHase from Bradyrhizobium elkanii~~, ~~which is a nitrogen-fixing bacterial symbiont of legume plants, was determined at~~ 1.7 A ~~resolution~~, ~~showing~~ the ~~domain organization (substrate-binding domain~~, ~~NAD(+) cofactor-binding domain and dimerization domain)~~ of the subunits. The ~~protein crystallized~~ in ~~its biologically relevant tetrameric form, with three~~ subunits in a closed conformation ~~enforced by complex formation with~~ the Ado ~~product~~ of the ~~enzymatic reaction~~. The ~~fourth~~ subunit is ligand~~-free and has~~ an open ~~conformation. The BeSAHase structure therefore provides~~ a ~~unique snapshot~~ of the ~~domain movement~~ of the ~~enzyme induced by~~ the ~~binding of its natural ligands~~.	+	S-Adenosyl-l-homocysteine hydrolase (SAHase) from the symbiotic bacterium Bradyrhizobium elkanii (BeSAHase) was crystallized in four ligand complexes with (i) mixed adenosine (Ado) and cordycepin (Cord; 3'-deoxyadenosine), (ii) adenine (Ade), (iii) Ado and (iv) mixed 2'-deoxyadenosine (2'-dAdo) and Ade. The crystal structures were solved at resolutions of 1.84, 1.95, 1.95 and 1.54 A, respectively. Only the Ade complex crystallized with a dimer in the asymmetric unit, while all of the other complexes formed a crystallographically independent tetrameric assembly. In the Ado/Cord complex, adenosine is found in three subunits while the fourth subunit has cordycepin bound in the active site. In the Ade and Ado complexes only these ligand molecules are present in the active sites. The 2'-dAdo/Ade complex has Ade bound in two subunits and 2'-dAdo bound in the other two subunits. The BeSAHase fold adopted a closed conformation in the complexes with Ado, Ade and 2'-dAdo, and a semi-open conformation when cordycepin occupied the active site. An SAHase-specific molecular gate, consisting of residues His342 and Phe343, behaves differently in the different complexes, but there is no simple correlation with the ligand type. Additional small-angle X-ray scattering (SAXS) experiments confirm the tetrameric state of the protein in solution. The main conclusions from this work are (i) that the SAHase subunit does not simply oscillate between two discrete conformational open/closed states in correlation with the absence/presence of a ligand in the active site, but can also assume an intermediate form for some ligands; (ii) that the shut/open state of the molecular gate in the access channel to the active site is not correlated in a simple way with the open/closed subunit conformation or empty/occupied status of the active site, but that a variety of states are possible even for the same ligand; (iii) that a cation (typically sodium) coordinated in an intersubunit loop rigidifies a molecular hinge and thus stabilizes the closed conformation; (iv) that BeSAHase in solution is a tetramer, consistent with the model derived from crystallography.

-	~~An enzyme captured in two conformational states: crystal structure~~ of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.,Manszewski T, ~~Singh~~ K~~, Imiolczyk B~~, Jaskolski M ~~Acta Crystallogr D Biol Crystallogr~~. ~~2015 Dec 1~~;71(Pt 12):~~2422~~-32. doi:, 10.1107/~~S1399004715018659~~. ~~Epub 2015 Nov 26~~. PMID:~~26627650~~<ref>PMID:~~26627650~~</ref>	+	Crystallographic and SAXS studies of S-adenosyl-l-homocysteine hydrolase from Bradyrhizobium elkanii.,Manszewski T, Szpotkowski K, Jaskolski M IUCrJ. 2017 Apr 10;4(Pt 3):271-282. doi: 10.1107/S2052252517002433. eCollection, 2017 May 1. PMID:28512574<ref>PMID:28512574</ref>

	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>

OCA at 12:51, 10 May 2017

OCA — Wed, 10 May 2017 12:51:56 GMT

←Older revision		Revision as of 12:51, 10 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5m66 is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine==
		+	<StructureSection load='5m66' size='340' side='right' caption='[[5m66]], [[Resolution\|resolution]] 1.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5m66]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M66 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lvc\|4lvc]], [[3ond\|3ond]], [[3one\|3one]], [[3onf\|3onf]], [[1a7a\|1a7a]], [[1v8b\|1v8b]], [[3ce6\|3ce6]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m66 OCA], [http://pdbe.org/5m66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m66 RCSB], [http://www.ebi.ac.uk/pdbsum/5m66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m66 ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	S-Adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM, S-adenosyl-L-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase. The crystal structure of BeSAHase, an SAHase from Bradyrhizobium elkanii, which is a nitrogen-fixing bacterial symbiont of legume plants, was determined at 1.7 A resolution, showing the domain organization (substrate-binding domain, NAD(+) cofactor-binding domain and dimerization domain) of the subunits. The protein crystallized in its biologically relevant tetrameric form, with three subunits in a closed conformation enforced by complex formation with the Ado product of the enzymatic reaction. The fourth subunit is ligand-free and has an open conformation. The BeSAHase structure therefore provides a unique snapshot of the domain movement of the enzyme induced by the binding of its natural ligands.

-	~~Authors~~: ~~Manszewski~~, T., ~~Jaskolski~~, M.	+	An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.,Manszewski T, Singh K, Imiolczyk B, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2422-32. doi:, 10.1107/S1399004715018659. Epub 2015 Nov 26. PMID:26627650<ref>PMID:26627650</ref>

-	~~Description: Crystal structure~~ of S-~~adenosyl~~-~~L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	[[Category: ~~Manszewski, T~~]]	+	<div class="pdbe-citations 5m66" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Adenosylhomocysteinase]]
	[[Category: Jaskolski, M]]		[[Category: Jaskolski, M]]
		+	[[Category: Manszewski, T]]
		+	[[Category: Adenosine]]
		+	[[Category: Conformational transition]]
		+	[[Category: Hydrolase]]
		+	[[Category: Molecular gate]]
		+	[[Category: Nad]]
		+	[[Category: Nitrogen fixation]]
		+	[[Category: Sah]]
		+	[[Category: Sahase]]
		+	[[Category: Sam-dependent methylation]]
		+	[[Category: Symbiotic bacteria]]

OCA at 16:25, 9 December 2016

OCA — Fri, 09 Dec 2016 16:25:09 GMT

←Older revision		Revision as of 16:25, 9 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5m66 is ON HOLD	+	The entry 5m66 is ON HOLD until Paper Publication

	Authors: Manszewski, T., Jaskolski, M.		Authors: Manszewski, T., Jaskolski, M.

OCA: Protected "5m66" [edit=sysop:move=sysop]

OCA — Wed, 02 Nov 2016 16:02:31 GMT

Protected "5m66" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:02, 2 November 2016

OCA: New page: '''Unreleased structure''' The entry 5m66 is ON HOLD Authors: Manszewski, T., Jaskolski, M. Description: Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium el...

OCA — Wed, 02 Nov 2016 16:02:29 GMT

New page: '''Unreleased structure''' The entry 5m66 is ON HOLD Authors: Manszewski, T., Jaskolski, M. Description: Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium el...

New page

'''Unreleased structure'''

The entry 5m66 is ON HOLD

Authors: Manszewski, T., Jaskolski, M.

Description: Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine
[[Category: Unreleased Structures]]
[[Category: Manszewski, T]]
[[Category: Jaskolski, M]]