3hhp: Difference between revisions
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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=3hhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hhp RCSB], [http://www.ebi.ac.uk/pdbsum/3hhp 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=3hhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hhp RCSB], [http://www.ebi.ac.uk/pdbsum/3hhp PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://www.uniprot.org/uniprot/MDH_ECOLI MDH_ECOLI]] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_01516] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 15:35, 25 December 2014
Malate dehydrogenase open conformationMalate dehydrogenase open conformation
Structural highlights
Function[MDH_ECOLI] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_01516] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 A resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 A, beta = 102.2 degrees. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (R(free) = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered. Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution.,Zaitseva J, Meneely KM, Lamb AL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):866-9. Epub 2009 Aug 20. PMID:19724119[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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