Structure of PDB 3gvi Chain F

Receptor sequence
>3gviF (length=314) Species: 359391 (Brucella abortus 2308) [Search protein sequence]
ARNKIALIGSGMIGGTLAHLAGLKELGDVVLFDIAEGTPQGKGLDIAESS
PVDGFDAKFTGANDYAAIEGADVVIVTAGVPRKDDLLGINLKVMEQVGAG
IKKYAPEAFVICITNPLDAMVWALQKFSGLPAHKVVGMAGVLDSARFRYF
LSEEFNVSVEDVTVFVLGGHGDSMVPLARYSTVAGIPLPDLVKMGWTSQD
KLDKIIQRTRDGGAEIVGLLKTGSAFYAPAASAIQMAESYLKDKKRVLPV
AAQLSGQYGVKDMYVGVPTVIGANGVERIIEIDLDKDEKAQFDKSVASVA
GLCEACIGIAPSLK
3D structure
PDB3gvi Crystal structure of Lactate/malate dehydrogenase from Brucella melitensis in complex with ADP
ChainF
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D149 R152 H176
Catalytic site (residue number reindexed from 1) D143 R146 H170
Enzyme Commision number 1.1.1.37: malate dehydrogenase.
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 ADP F G12 M13 I14 D34 I35 A79 G80 V99 G11 M12 I13 D33 I34 A78 G79 V93
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0030060 L-malate dehydrogenase (NAD+) activity
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0006099 tricarboxylic acid cycle
GO:0019752 carboxylic acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gvi, PDBe:3gvi, PDBj:3gvi
PDBsum3gvi
PubMed
UniProtQ2YLR9|MDH_BRUA2 Malate dehydrogenase (Gene Name=mdh)

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