Structure of PDB 1bmd Chain A

Receptor sequence

>1bmdA (length=327) Species: 274 (Thermus thermophilus)

MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKAL
EGVVMELEDCAFPLLAGLEATDDPDVAFKDADYALLVGAAPRKAGMERRD
LLQVNGKIFTEQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPR
NFTAMTRLDHNRAKAQLAKKTGTGVDRIRRMTVWGNHSSTMFPDLFHAEV
DGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIR
DWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEIN
EFARKRMEITAQELLDEMEQVKALGLI

3D structure

• PDB: 1bmd Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D158 N185 H186
• Catalytic site (residue number reindexed from 1): D159 N186 H187
• 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	G10 G13 Q14 I15 E41 I42 V86 G87 V128 G129 N130 M154 H186	G11 G14 Q15 I16 E42 I43 V87 G88 V129 G130 N131 M155 H187

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:1bmd, PDBe:1bmd, PDBj:1bmd
• PDBsum: 1bmd
• PubMed: 8471603
• UniProt: P10584|MDH_THETH Malate dehydrogenase (Gene Name=mdh)