Structure of PDB 2dvm Chain D

Receptor sequence
>2dvmD (length=436) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
IREKALEFHKNNFPGNGKIEVIPKVSLESREELTLAYTPGVAEPCKEIAR
DPGKVYEYTSKGNLVAVVSDGSRILGLGNIGPLAGLPVMEGKALLFKRFG
GVDAFPIMIKEQEPNKFIDIVKAIAPTFGGINLEDIASPKCFYILERLRE
ELDIPVFHDDQQGTAAVVLAGLLNALKVVGKKISEITLALFGAGAAGFAT
LRILTEAGVKPENVRVVELVNGKPRILTSDLDLEKLFPYRGWLLKKTNGE
NIEGGPQEALKDADVLISFTRPGPGVIKPQWIEKMNEDAIVFPLANPVPE
ILPEEAKKAGARIVATGRSDYPNQINNLLGFPGIFRGALDVRARTITDSM
IIAAAKAIASIVEEPSEENIIPSPLNPIVYAREARAVAEEAMKEGVARTK
VKGEWVEEHTIRLIEFYENVIAPINKKRREYSKAIT
3D structure
PDB2dvm NAD complex structure of PH1275 protein from Pyrococcus horikoshii
ChainD
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y38 R74 K93 E135 D136 D160 D161 N297
Catalytic site (residue number reindexed from 1) Y37 R73 K92 E134 D135 D159 D160 N296
Enzyme Commision number 1.1.1.38: malate dehydrogenase (oxaloacetate-decarboxylating).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD D R74 T165 G195 A196 A197 V218 E219 L220 P225 F270 T271 L295 N297 R73 T164 G194 A195 A196 V217 E218 L219 P224 F269 T270 L294 N296
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004470 malic enzyme activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding

View graph for
Molecular Function
External links
PDB RCSB:2dvm, PDBe:2dvm, PDBj:2dvm
PDBsum2dvm
PubMed
UniProtO59029

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