Structure of PDB 1b8u Chain A

Receptor sequence

>1b8uA (length=327) Species: 87645 (Aquaspirillum arcticum)

KTPMRVAVTGAAGQICYSLLFRIANGDMLGKDQPVILQLLEIPNEKAQKA
LQGVMMEIDDCAFPLLAGMTAHADPMTAFKDADVALLVGARPRGPGMERK
DLLEANAQIFTVQGKAIDAVASRNIKVLVVGNPANTNAYIAMKSAPSLPA
KNFTAMLRLDHNRALSQIAAKTGKPVSSIEKLFVWGNHSPTMYADYRYAQ
IDGASVKDMINDDAWNRDTFLPTVGKRGAAIIDARGVSSAASAANAAIDH
IHDWVLGTAGKWTTMGIPSDGSYGIPEGVIFGFPVTTENGEYKIVQGLSI
DAFSQERINVTLNELLEEQNGVQHLLG

3D structure

• PDB: 1b8u Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum.
• Chain: A
• Resolution: 2.5 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	OAA	A	R165 H190 G227 K228 G230	R163 H188 G225 K226 G228
BS02	NAD	A	T11 G12 G15 Q16 I17 E43 I44 V90 Q115 V132 G133 N134 M158 H190	T9 G10 G13 Q14 I15 E41 I42 V88 Q113 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:1b8u, PDBe:1b8u, PDBj:1b8u
• PDBsum: 1b8u
• PubMed: 10206992
• UniProt: Q9ZF99|MDH_AQUAR Malate dehydrogenase (Gene Name=mdh)