3vvm - Revision history

OCA at 12:39, 8 November 2023

OCA — Wed, 08 Nov 2023 12:39:37 GMT

←Older revision		Revision as of 12:39, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3vvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VVM FirstGlance]. <br>		<table><tr><td colspan='2'>[[3vvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VVM FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[3vvl\|3vvl]]</div></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]] 1.7Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">dcsE, metX ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=58340 Streptomyces lavendulae subsp. lavendulae])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [https://pdbe.org/3vvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [https://www.ebi.ac.uk/pdbsum/3vvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvm 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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [https://pdbe.org/3vvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [https://www.ebi.ac.uk/pdbsum/3vvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvm ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/DCSE_STRLA DCSE_STRLA] Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine.<ref>PMID:20086163</ref> <ref>PMID:23396912</ref>
	<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: Homoserine O-acetyltransferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Streptomyces lavendulae subsp. lavendulae]]		[[Category: Streptomyces lavendulae subsp. lavendulae]]
-	[[Category: Kumagai, T]]	+	[[Category: Kumagai T]]
-	[[Category: Matoba, Y]]	+	[[Category: Matoba Y]]
-	[[Category: Noda, M]]	+	[[Category: Noda M]]
-	[[Category: Oda, K]]	+	[[Category: Oda K]]
-	[[Category: Sugiyama, M]]	+	[[Category: Sugiyama M]]
-	~~[[Category: Alpha/beta hydrolase domain]]~~	+
-	~~[[Category: D-cycloserine]]~~	+
-	~~[[Category: L-serine-o-acetyltransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 19:06, 27 July 2022

OCA — Wed, 27 Jul 2022 19:06:36 GMT

←Older revision		Revision as of 19:06, 27 July 2022
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	==Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway==		==Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway==
-	<StructureSection load='3vvm' size='340' side='right' caption='[[3vvm]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='3vvm' size='340' side='right'caption='[[3vvm]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vvm]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3VVM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VVM FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vvl\|3vvl]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vvl\|3vvl]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dcsE, metX ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=58340 Streptomyces lavendulae subsp. lavendulae])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dcsE, metX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=58340 Streptomyces lavendulae subsp. lavendulae])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [~~http~~://pdbe.org/3vvm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3vvm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvm 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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [https://pdbe.org/3vvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [https://www.ebi.ac.uk/pdbsum/3vvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvm ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Homoserine O-acetyltransferase]]		[[Category: Homoserine O-acetyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Streptomyces lavendulae subsp. lavendulae]]		[[Category: Streptomyces lavendulae subsp. lavendulae]]
	[[Category: Kumagai, T]]		[[Category: Kumagai, T]]

OCA at 10:19, 4 August 2016

OCA — Thu, 04 Aug 2016 10:19:50 GMT

←Older revision		Revision as of 10:19, 4 August 2016
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		+
	==Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway==		==Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway==
	<StructureSection load='3vvm' size='340' side='right' caption='[[3vvm]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='3vvm' size='340' side='right' caption='[[3vvm]], [[Resolution\|resolution]] 1.70Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dcsE, metX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=58340 Streptomyces lavendulae subsp. lavendulae])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dcsE, metX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=58340 Streptomyces lavendulae subsp. lavendulae])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [http://www.ebi.ac.uk/pdbsum/3vvm 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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [http://pdbe.org/3vvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [http://www.ebi.ac.uk/pdbsum/3vvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvm 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 3vvm" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:09, 21 December 2014

OCA — Sun, 21 Dec 2014 07:09:15 GMT

←Older revision		Revision as of 07:09, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3vvm\| PDB=3vvm \| SCENE= }}~~	+	==Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway==
-	===Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway===	+	<StructureSection load='3vvm' size='340' side='right' caption='[[3vvm]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23396912}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VVM FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vvl\|3vvl]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">dcsE, metX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=58340 Streptomyces lavendulae subsp. lavendulae])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </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=3vvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vvm RCSB], [http://www.ebi.ac.uk/pdbsum/3vvm PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DcsE, one of the enzymes found in the d-cycloserine biosynthetic pathway, displays a high sequence homology to l-homoserine O-acetyltransferase (HAT), but it prefers l-serine over l-homoserine as the substrate. To clarify the substrate specificity, in the present study we determined the crystal structure of DcsE at a 1.81 A resolution, showing that the overall structure of DcsE is similar to that of HAT, whereas a turn region to form an oxyanion hole is obviously different between DcsE and HAT: in detail, the first and last residues in the turn of DcsE are Gly(52) and Pro(55), respectively, but those of HAT are Ala and Gly. In addition, more water molecules were laid on one side of the turn region of DcsE than on that of HAT, and a robust hydrogen-bonding network was formed only in DcsE. We created a HAT-like mutant of DcsE in which Gly(52) and Pro(55) were replaced by Ala and Gly, respectively, showing that the mutant acetylates l-homoserine but scarcely l-serine. The crystal structure of the mutant DcsE shows that the active site, including the turn and its surrounding waters, is similar to that of HAT. These findings suggest that a methyl group of the first residue in the turn of HAT plays a role in excluding the binding of l-serine to the substrate-binding pocket. In contrast, the side chain of the last residue in the turn of DcsE may need to form an extensive hydrogen-bonding network on the turn, which interferes with the binding of l-homoserine.

-	~~==About this Structure==~~	+	Crystallographic study to determine the substrate specificity on an L-serine-acetylating enzyme found in the D-cycloserine biosynthetic pathway.,Oda K, Matoba Y, Kumagai T, Noda M, Sugiyama M J Bacteriol. 2013 Feb 8. PMID:23396912<ref>PMID:23396912</ref>
-	~~[[3vvm]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Streptomyces_lavendulae_subsp~~.~~_lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023396912</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homoserine O-acetyltransferase]]		[[Category: Homoserine O-acetyltransferase]]
	[[Category: Streptomyces lavendulae subsp. lavendulae]]		[[Category: Streptomyces lavendulae subsp. lavendulae]]
-	[[Category: Kumagai, T.]]	+	[[Category: Kumagai, T]]
-	[[Category: Matoba, Y.]]	+	[[Category: Matoba, Y]]
-	[[Category: Noda, M.]]	+	[[Category: Noda, M]]
-	[[Category: Oda, K.]]	+	[[Category: Oda, K]]
-	[[Category: Sugiyama, M.]]	+	[[Category: Sugiyama, M]]
	[[Category: Alpha/beta hydrolase domain]]		[[Category: Alpha/beta hydrolase domain]]
	[[Category: D-cycloserine]]		[[Category: D-cycloserine]]
	[[Category: L-serine-o-acetyltransferase]]		[[Category: L-serine-o-acetyltransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 18:21, 19 June 2013

OCA — Wed, 19 Jun 2013 18:21:20 GMT

←Older revision		Revision as of 18:21, 19 June 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3vvm\| PDB=3vvm \| SCENE= }}
		+	===Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway===
		+	{{ABSTRACT_PUBMED_23396912}}

-	~~The entry~~ 3vvm is ~~ON HOLD until Paper Publication~~	+	==About this Structure==
		+	[[3vvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVM OCA].

-	~~Authors~~: ~~Oda, K~~.~~, Matoba, Y.,~~ Kumagai, T., Noda, M., Sugiyama, M.	+	==Reference==
-		+	<ref group="xtra">PMID:023396912</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Crystal structure of G52A~~-~~P55G mutant of~~ L-serine-O-acetyltransferase ~~found in D-cycloserine biosynthetic pathway~~	+	[[Category: Homoserine O-acetyltransferase]]
		+	[[Category: Streptomyces lavendulae subsp. lavendulae]]
		+	[[Category: Kumagai, T.]]
		+	[[Category: Matoba, Y.]]
		+	[[Category: Noda, M.]]
		+	[[Category: Oda, K.]]
		+	[[Category: Sugiyama, M.]]
		+	[[Category: Alpha/beta hydrolase domain]]
		+	[[Category: D-cycloserine]]
		+	[[Category: L-serine-o-acetyltransferase]]
		+	[[Category: Transferase]]

OCA at 06:40, 10 October 2012

OCA — Wed, 10 Oct 2012 06:40:06 GMT

←Older revision		Revision as of 06:40, 10 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Oda, K., Matoba, Y., Kumagai, T., Noda, M., Sugiyama, M.		Authors: Oda, K., Matoba, Y., Kumagai, T., Noda, M., Sugiyama, M.

	Description: Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway		Description: Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway

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

OCA — Wed, 01 Aug 2012 05:15:24 GMT

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

←Older revision

Revision as of 05:15, 1 August 2012

OCA: New page: '''Unreleased structure''' The entry 3vvm is ON HOLD Authors: Oda, K., Matoba, Y., Kumagai, T., Noda, M., Sugiyama, M. Description: Crystal structure of G52A-P55G mutant of L-serine-O-...

OCA — Wed, 01 Aug 2012 05:15:23 GMT

New page: '''Unreleased structure''' The entry 3vvm is ON HOLD Authors: Oda, K., Matoba, Y., Kumagai, T., Noda, M., Sugiyama, M. Description: Crystal structure of G52A-P55G mutant of L-serine-O-...

New page

'''Unreleased structure'''

The entry 3vvm is ON HOLD

Authors: Oda, K., Matoba, Y., Kumagai, T., Noda, M., Sugiyama, M.

Description: Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway