Structure of PDB 1bdm Chain B

Receptor sequence

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

MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKAL
EGVVMELEDCAFPLLAGLEATDDPDVAFKDADYALLVGAAPRKAGMERRD
LLQVNGKIFTEQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPR
NFTAMTRLDHNRAKAQLAKKTGTGVDRIRRMTVWGNHSSIMFPDLFHAEV
DGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIR
DWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEIN
EFARKRMEITAQELLDEMEQVKALGLI

3D structure

• PDB: 1bdm Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D158 H186
• Catalytic site (residue number reindexed from 1): D159 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	NAX	B	G10 G13 Q14 I15 E41 I42 V86 G87 I107 V128 G129 N130 M154 H186	G11 G14 Q15 I16 E42 I43 V87 G88 I108 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:1bdm, PDBe:1bdm, PDBj:1bdm
• PDBsum: 1bdm
• PubMed: 8471603
• UniProt: P10584|MDH_THETH Malate dehydrogenase (Gene Name=mdh)