Structure of PDB 1b8v Chain A

Receptor sequence

>1b8vA (length=327) Species: 87645 (Aquaspirillum arcticum)

KTPMRVAVTGAAGQICYSLLFRIANGDMLGKDQPVILQLLEIPNEKAQKA
LQGVMMEIDDCAFPLLAGMTAHADPMTAFKDADVALLVGARPRGPGMERK
DLLEANAQIFTVQGKAIDAVASRNIKVLVVGNPANTNAYIAMKSAPSLPA
KNFTAMLRLDHNRALSQIAAKTGKPVSSIEKLFVWGNHSPTMYADYRYAQ
IDGASVKDMINDDAWNRDTFLPTVGKRGAAIIDARGVSSAASAANAAIDH
IHDWVLGTAGKWTTMGIPSDGSYGIPEGVIFGFPVTTENGEYKIVQGLSI
DAFSQERINVTLNELLEEQNGVQHLLG

3D structure

• PDB: 1b8v Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum.
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D162 H190
• Catalytic site (residue number reindexed from 1): D160 H188
• 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 G15 Q16 I17 E43 I44 V90 G91 V132 G133 N134 M158 H190	G10 G13 Q14 I15 E41 I42 V88 G89 V130 G131 N132 M156 H188

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0016491 oxidoreductase activity
• GO:0016615 malate dehydrogenase 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:0006099 tricarboxylic acid cycle
• GO:0006107 oxaloacetate metabolic process
• GO:0006108 malate metabolic process
• GO:0006734 NADH metabolic process
• GO:0019752 carboxylic acid metabolic process

External links

• PDB: RCSB:1b8v, PDBe:1b8v, PDBj:1b8v
• PDBsum: 1b8v
• PubMed: 10206992
• UniProt: Q9ZF99|MDH_AQUAR Malate dehydrogenase (Gene Name=mdh)