3vph - Revision history

OCA at 12:31, 8 November 2023

2023-11-08T12:31:17Z

←Older revision		Revision as of 12:31, 8 November 2023
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	<StructureSection load='3vph' size='340' side='right'caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3vph' size='340' side='right'caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vph]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"thermus_caldophilus"_taguchi_et_al._1983 "thermus~~ caldophilus~~" taguchi et al. 1983~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vph]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</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]] 2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vpg\|3vpg]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ldh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272 "Thermus caldophilus" Taguchi et al. 1983])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [https://pdbe.org/3vph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [https://www.ebi.ac.uk/pdbsum/3vph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vph 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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [https://pdbe.org/3vph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [https://www.ebi.ac.uk/pdbsum/3vph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vph ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/LDH_THECA LDH_THECA]
	<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: Thermus caldophilus taguchi et al. 1983]]
-	[[Category: L-lactate dehydrogenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arai, K]]	+	[[Category: Thermus caldophilus]]
-	[[Category: Fushinobu, S]]	+	[[Category: Arai K]]
-	[[Category: Miyanaga, A]]	+	[[Category: Fushinobu S]]
-	[[Category: Ohno, T]]	+	[[Category: Miyanaga A]]
-	[[Category: Taguchi, H]]	+	[[Category: Ohno T]]
-	~~[[Category: Dehydrogenase]]~~	+	[[Category: Taguchi H]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Rossmann fold~~]]	+

OCA at 18:57, 27 July 2022

2022-07-27T18:57:13Z

←Older revision		Revision as of 18:57, 27 July 2022
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	==L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP==		==L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP==
-	<StructureSection load='3vph' size='340' side='right' caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='3vph' size='340' side='right'caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vph]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"thermus_caldophilus"_taguchi_et_al._1983 "thermus caldophilus" taguchi et al. 1983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3VPH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vph]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermus_caldophilus"_taguchi_et_al._1983 "thermus caldophilus" taguchi et al. 1983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vpg\|3vpg]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vpg\|3vpg]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ldh ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272 "Thermus caldophilus" Taguchi et al. 1983])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ldh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272 "Thermus caldophilus" Taguchi et al. 1983])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [~~http~~://pdbe.org/3vph PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3vph PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3vph 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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [https://pdbe.org/3vph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [https://www.ebi.ac.uk/pdbsum/3vph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vph ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Lactate ~~Dehydrogenase~~\|Lactate ~~Dehydrogenase~~]]	+	*[[Lactate dehydrogenase 3D structures\|Lactate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 28:
	[[Category: Thermus caldophilus taguchi et al. 1983]]		[[Category: Thermus caldophilus taguchi et al. 1983]]
	[[Category: L-lactate dehydrogenase]]		[[Category: L-lactate dehydrogenase]]
		+	[[Category: Large Structures]]
	[[Category: Arai, K]]		[[Category: Arai, K]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]

OCA at 16:31, 11 August 2016

2016-08-11T16:31:41Z

←Older revision		Revision as of 16:31, 11 August 2016
Line 1:		Line 1:
		+
	==L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP==		==L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP==
	<StructureSection load='3vph' size='340' side='right' caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3vph' size='340' side='right' caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ldh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272 "Thermus caldophilus" Taguchi et al. 1983])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ldh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272 "Thermus caldophilus" Taguchi et al. 1983])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [http://www.ebi.ac.uk/pdbsum/3vph 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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [http://pdbe.org/3vph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [http://www.ebi.ac.uk/pdbsum/3vph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vph ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	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 3vph" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 10:42, 20 January 2015

2015-01-20T10:42:29Z

←Older revision		Revision as of 10:42, 20 January 2015
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	[[Category: Thermus caldophilus taguchi et al. 1983]]		[[Category: Thermus caldophilus taguchi et al. 1983]]
	[[Category: L-lactate dehydrogenase]]		[[Category: L-lactate dehydrogenase]]
-	[[Category: Arai, K.]]	+	[[Category: Arai, K]]
-	[[Category: Fushinobu, S.]]	+	[[Category: Fushinobu, S]]
-	[[Category: Miyanaga, A.]]	+	[[Category: Miyanaga, A]]
-	[[Category: Ohno, T.]]	+	[[Category: Ohno, T]]
-	[[Category: Taguchi, H.]]	+	[[Category: Taguchi, H]]
	[[Category: Dehydrogenase]]		[[Category: Dehydrogenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]

OCA at 05:55, 8 October 2014

2014-10-08T05:55:10Z

←Older revision		Revision as of 05:55, 8 October 2014
Line 1:		Line 1:
-	[[~~Image:~~3vph.~~jpg~~\|~~left~~\|~~200px~~]]	+	==L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP==
		+	<StructureSection load='3vph' size='340' side='right' caption='[[3vph]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3vph]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermus_caldophilus"_taguchi_et_al._1983 "thermus caldophilus" taguchi et al. 1983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VPH FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vpg\|3vpg]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ldh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272 "Thermus caldophilus" Taguchi et al. 1983])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </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=3vph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vph RCSB], [http://www.ebi.ac.uk/pdbsum/3vph PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	For Thermus caldophilus L-lactate dehydrogenase (TcLDH), fructose 1,6-bisphosphate (FBP) reduced the pyruvate S0.5 value 103-fold and increased the Vmax value 4-fold at 30 degrees C and pH 7.0, indicating that TcLDH has a much more T state-sided allosteric equilibrium than the Thermus thermophilus enzyme (TtLDH), which has only two amino acid replacements, A154G and H179Y. The inactive (T) and active (R) state structures of TcLDH were determined at 1.8 and 2.0 A resolution, respectively. The structures indicated that two mobile regions, MR1 (positions 172 to 185) and MR2 (212 to 220), form a compact core for allosteric motion, and His179 of MR1 forms constitutive hydrogen bonds with MR2. The Q4(R) mutation, which comprises the L67E, H68D, E178K and A235R replacements increased Vmax 4-fold, but reduced pyruvate S0.5 only 5-fold in the reaction without FBP. In contrast, the P2 mutation, comprising the R173Q and R216L replacements, did not markedly increase Vmax, but 102-reduced pyruvate S0.5, and additively increased the FBP-independent activity of the Q4(R) enzyme. The two types of mutation consistently increased the thermal stability of the enzyme. The MR1-MR2 area is a positively charged cluster, and its center approaches another positively charged cluster (N-domain cluster) across the Q-axis subunit interface by 5 A, when the enzyme undergoes the T to R transition. Structural and kinetic analyses thus revealed the simple and unique allosteric machinery of TcLDH, where the MR1-MR2 area pivotally moves during the allosteric motion, and mediates the allosteric equilibrium through electrostatic repulsion within the protein molecule.

-	~~{{STRUCTURE_3vph\| PDB=3vph \| SCENE= }}~~	+	The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.,Ikehara Y, Arai K, Furukawa N, Ohno T, Miyake T, Fushinobu S, Nakajima M, Miyanaga A, Taguchi H J Biol Chem. 2014 Sep 25. pii: jbc.M114.599092. PMID:25258319<ref>PMID:25258319</ref>

-	~~===L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate~~, ~~NADH and FBP===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	==~~About this Structure~~==	+	*[[Lactate Dehydrogenase\|Lactate Dehydrogenase]]
-	[[~~3vph~~]] ~~is a 4 chain structure with sequence from~~ [~~http~~:~~//en.wikipedia.org/wiki/Thermus_caldophilus~~ Thermus caldophilus]. ~~Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA~~].	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Thermus caldophilus taguchi et al. 1983]]
	[[Category: L-lactate dehydrogenase]]		[[Category: L-lactate dehydrogenase]]
-	[[Category: Thermus caldophilus]]
	[[Category: Arai, K.]]		[[Category: Arai, K.]]
	[[Category: Fushinobu, S.]]		[[Category: Fushinobu, S.]]

OCA at 14:19, 6 March 2013

2013-03-06T14:19:20Z

←Older revision		Revision as of 14:19, 6 March 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3vph.jpg\|left\|200px]]

-	~~The entry~~ 3vph ~~is ON HOLD~~ ~~until Mar 01 2014~~	+	{{STRUCTURE_3vph\| PDB=3vph \| SCENE= }}

-	~~Authors: Arai~~, ~~K., Ohno, T., Miyanaga, A., Fushinobu, S., Taguchi, H.~~	+	===L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP===

-	~~Description~~: L-lactate dehydrogenase ~~from~~ Thermus caldophilus ~~GK24 complexed with oxamate~~, ~~NADH and FBP~~	+
		+	==About this Structure==
		+	[[3vph]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPH OCA].
		+	[[Category: L-lactate dehydrogenase]]
		+	[[Category: Thermus caldophilus]]
		+	[[Category: Arai, K.]]
		+	[[Category: Fushinobu, S.]]
		+	[[Category: Miyanaga, A.]]
		+	[[Category: Ohno, T.]]
		+	[[Category: Taguchi, H.]]
		+	[[Category: Dehydrogenase]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Rossmann fold]]

OCA at 07:06, 21 March 2012

2012-03-21T07:06:34Z

←Older revision		Revision as of 07:06, 21 March 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3vph is ON HOLD	+	The entry 3vph is ON HOLD until Mar 01 2014

-	Authors: Arai, K., ~~Miyanaga~~, A., ~~Uchikoba~~, H., Fushinobu, S., Taguchi, H.	+	Authors: Arai, K., Ohno, T., Miyanaga, A., Fushinobu, S., Taguchi, H.

	Description: L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP		Description: L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP

OCA at 06:05, 14 March 2012

2012-03-14T06:05:27Z

←Older revision		Revision as of 06:05, 14 March 2012
Line 3:		Line 3:
	The entry 3vph is ON HOLD		The entry 3vph is ON HOLD

-	Authors: Arai, K~~, Ohno, T~~, Miyanaga, A, Fushinobu, S , Taguchi, H	+	Authors: Arai, K., Miyanaga, A., Uchikoba, H., Fushinobu, S., Taguchi, H.

	Description: L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP		Description: L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP

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

2012-03-08T05:20:34Z

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

←Older revision

Revision as of 05:20, 8 March 2012

OCA: New page: '''Unreleased structure''' The entry 3vph is ON HOLD Authors: Arai, K, Ohno, T, Miyanaga, A, Fushinobu, S , Taguchi, H Description: L-lactate dehydrogenase from Thermus caldophilus GK2...

2012-03-08T05:20:33Z

New page: '''Unreleased structure''' The entry 3vph is ON HOLD Authors: Arai, K, Ohno, T, Miyanaga, A, Fushinobu, S , Taguchi, H Description: L-lactate dehydrogenase from Thermus caldophilus GK2...

New page

'''Unreleased structure'''

The entry 3vph is ON HOLD

Authors: Arai, K, Ohno, T, Miyanaga, A, Fushinobu, S , Taguchi, H

Description: L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP