Structure of PDB 5ujk Chain A

Receptor sequence
>5ujkA (length=315) Species: 408 (Methylorubrum extorquens) [Search protein sequence]
ARSKIALIGAGQIGGTLAHLAGLKELGDVVLFDIVDGVPQGKALDIAESA
PVDGFDAKYSGASDYSAIAGADVVIVTAGVPRKPGMSRDDLIGINLKVME
AVGAGIKEHAPDAFVICITNPLDAMVWALQKFSGLPTNKVVGMAGVLDSA
RFRHFLAEEFGVSVEDVTAFVLGGHGDDMVPLTRYSTVAGVPLTDLVKLG
WTTQEKLDAMVERTRKGGGEIVNLLKTGSAFYAPAASAIAMAESYLRDKK
RVLPCAAYLDGQYGIDGLYVGVPVVIGENGVERVLEVTFNDDEKAMFEKS
VNSVKGLIEACKSVN
3D structure
PDB5ujk Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase.
ChainA
Resolution1.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R89 D149 R152 H176
Catalytic site (residue number reindexed from 1) R88 D148 R151 H175
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 NAD A G12 Q13 I14 D34 I35 T78 A79 G80 V99 I119 N121 M144 L148 H176 G11 Q12 I13 D33 I34 T77 A78 G79 V98 I118 N120 M143 L147 H175
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:5ujk, PDBe:5ujk, PDBj:5ujk
PDBsum5ujk
PubMed30279311
UniProtQ84FY8|MDH_METEA Malate dehydrogenase (Gene Name=mdh)

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