5e4r - Revision history

OCA at 06:12, 5 July 2023

OCA — Wed, 05 Jul 2023 06:12:52 GMT

←Older revision		Revision as of 06:12, 5 July 2023
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	<StructureSection load='5e4r' size='340' side='right'caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='5e4r' size='340' side='right'caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ignaa Ignaa~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5E4R FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ignisphaera_aggregans_DSM_17230 Ignisphaera aggregans DSM 17230]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E4R FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.94Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ilvC, Igag_1561 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=583356 IGNAA])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [https://pdbe.org/5e4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [https://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r 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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [~~http~~://pdbe.org/5e4r PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/ILVC_IGNAA ILVC_IGNAA] Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate.<ref>PMID:25172159</ref> <ref>PMID:26644020</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: ~~Ignaa]]~~	+	[[Category: Ignisphaera aggregans DSM 17230]]
-	~~[[Category: Ketol-acid reductoisomerase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arnold~~, F H~~]]	+	[[Category: Arnold FH]]
-	[[Category: Brinkmann-Chen, S]]	+	[[Category: Brinkmann-Chen S]]
-	[[Category: Buller~~, A R~~]]	+	[[Category: Buller AR]]
-	[[Category: Cahn~~, J K.B]]~~	+	[[Category: Cahn JKB]]
-	~~[[Category: Chimera protein]]~~	+
-	~~[[Category: Ketol-acid reductiosomerase]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Protein engineering]]~~	+
-	~~[[Category: Protein knot]]~~	+
-	~~[[Category: Psuedodimer~~]]	+

OCA at 06:44, 22 April 2020

OCA — Wed, 22 Apr 2020 06:44:06 GMT

←Older revision		Revision as of 06:44, 22 April 2020
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	==Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD==		==Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD==
-	<StructureSection load='5e4r' size='340' side='right' caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>	+	<StructureSection load='5e4r' size='340' side='right'caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5E4R FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ignaa Ignaa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E4R FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ilvC, Igag_1561 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=583356 IGNAA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r 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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	</div>		</div>
	<div class="pdbe-citations 5e4r" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5e4r" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ketol-acid reductoisomerase 3D structures\|Ketol-acid reductoisomerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ignaa]]
	[[Category: Ketol-acid reductoisomerase]]		[[Category: Ketol-acid reductoisomerase]]
		+	[[Category: Large Structures]]
	[[Category: Arnold, F H]]		[[Category: Arnold, F H]]
	[[Category: Brinkmann-Chen, S]]		[[Category: Brinkmann-Chen, S]]

OCA at 18:36, 12 July 2016

OCA — Tue, 12 Jul 2016 18:36:35 GMT

←Older revision		Revision as of 18:36, 12 July 2016
Line 1:		Line 1:
		+
	==Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD==		==Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD==
	<StructureSection load='5e4r' size='340' side='right' caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>		<StructureSection load='5e4r' size='340' side='right' caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r 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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4r ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:36, 30 December 2015

OCA — Wed, 30 Dec 2015 11:36:16 GMT

←Older revision		Revision as of 11:36, 30 December 2015
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	<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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r 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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The duplication of protein structural domains has been proposed as a common mechanism for the generation of new protein folds. A particularly interesting case is the class II ketol-acid reductoisomerase (KARI), which putatively arose from an ancestral class I KARI by duplication of the C-terminal domain and corresponding loss of obligate dimerization. As a result, the class II enzymes acquired a deeply embedded figure-of-eight knot. To test this evolutionary hypothesis we constructed a novel class II KARI by duplicating the C-terminal domain of a hyperthermostable class I KARI. The new protein is monomeric, as confirmed by gel filtration and x-ray crystallography, and has the deeply-knotted class II KARI fold. Surprisingly, its catalytic activity is nearly unchanged from the parent KARI. This provides strong evidence in support of domain duplication as the mechanism for the evolution of the class II KARI fold and demonstrates the ability of domain duplication to generate topological novelty in a function-neutral manner. This article is protected by copyright. All rights reserved.
		+
		+	Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases.,Cahn JK, Brinkmann-Chen S, Buller AR, Arnold FH Protein Sci. 2015 Dec 8. doi: 10.1002/pro.2852. PMID:26644020<ref>PMID:26644020</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5e4r" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:48, 23 December 2015

OCA — Wed, 23 Dec 2015 12:48:59 GMT

←Older revision		Revision as of 12:48, 23 December 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD==
-		+	<StructureSection load='5e4r' size='340' side='right' caption='[[5e4r]], [[Resolution\|resolution]] 1.94Å' scene=''>
-	~~The entry~~ 5e4r is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5e4r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E4R FirstGlance]. <br>
-	~~Authors~~: ~~Cahn, J~~.K.B., ~~Brinkmann~~-~~Chen~~, S., ~~Buller~~, A.R., ~~Arnold, F~~.H.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=40E:OXO(PROPAN-2-YLAMINO)ACETIC+ACID'>40E</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </span></td></tr>
-	~~Description~~: ~~Crystal structure of domain-duplicated synthetic~~ class ~~II ketol~~-~~acid reductoisomerase 2Ia_KARI~~-DD	+	<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=5e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4r OCA], [http://pdbe.org/5e4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e4r RCSB], [http://www.ebi.ac.uk/pdbsum/5e4r PDBsum]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
-	[[Category: ~~Buller~~, ~~A.R~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Ketol-acid reductoisomerase]]
		+	[[Category: Arnold, F H]]
	[[Category: Brinkmann-Chen, S]]		[[Category: Brinkmann-Chen, S]]
-	[[Category: Cahn, J.K.B]]	+	[[Category: Buller, A R]]
-	[[Category: ~~Arnold, F.H~~]]	+	[[Category: Cahn, J K.B]]
		+	[[Category: Chimera protein]]
		+	[[Category: Ketol-acid reductiosomerase]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Protein engineering]]
		+	[[Category: Protein knot]]
		+	[[Category: Psuedodimer]]

OCA at 11:38, 16 December 2015

OCA — Wed, 16 Dec 2015 11:38:21 GMT

←Older revision		Revision as of 11:38, 16 December 2015
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	Description: Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD		Description: Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Brinkmann-Chen, S]]
	[[Category: Buller, A.R]]		[[Category: Buller, A.R]]
		+	[[Category: Brinkmann-Chen, S]]
	[[Category: Cahn, J.K.B]]		[[Category: Cahn, J.K.B]]
	[[Category: Arnold, F.H]]		[[Category: Arnold, F.H]]

OCA: Protected "5e4r" [edit=sysop:move=sysop]

OCA — Fri, 16 Oct 2015 02:59:53 GMT

Protected "5e4r" [edit=sysop:move=sysop]

←Older revision

Revision as of 02:59, 16 October 2015

OCA: New page: '''Unreleased structure''' The entry 5e4r is ON HOLD Authors: Cahn, J.K.B., Brinkmann-Chen, S., Buller, A.R., Arnold, F.H. Description: Crystal structure of domain-duplicated synthetic...

OCA — Fri, 16 Oct 2015 02:59:52 GMT

New page: '''Unreleased structure''' The entry 5e4r is ON HOLD Authors: Cahn, J.K.B., Brinkmann-Chen, S., Buller, A.R., Arnold, F.H. Description: Crystal structure of domain-duplicated synthetic...

New page

'''Unreleased structure'''

The entry 5e4r is ON HOLD

Authors: Cahn, J.K.B., Brinkmann-Chen, S., Buller, A.R., Arnold, F.H.

Description: Crystal structure of domain-duplicated synthetic class II ketol-acid reductoisomerase 2Ia_KARI-DD
[[Category: Unreleased Structures]]
[[Category: Brinkmann-Chen, S]]
[[Category: Buller, A.R]]
[[Category: Cahn, J.K.B]]
[[Category: Arnold, F.H]]