Structure of PDB 1bdm Chain A

Receptor sequence
>1bdmA (length=317) Species: 274 (Thermus thermophilus) [Search protein sequence]
MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKAL
EGVVMELEDCAFPLLAGLEATDDPDVAFKDADYALLVGAAPLQVNGKIFT
EQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAMTRLDH
NRAKAQLAKKTGTGVDRIRRMTVWGNHSSIMFPDLFHAEVDGRPALELVD
MEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIRDWALGTPEGD
WVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEINEFARKRMEIT
AQELLDEMEQVKALGLI
3D structure
PDB1bdm Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D158 H186
Catalytic site (residue number reindexed from 1) D149 H177
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 A G10 G13 Q14 I15 E41 I42 V86 V128 G129 N130 M154 H186 G11 G14 Q15 I16 E42 I43 V87 V119 G120 N121 M145 H177
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1bdm, PDBe:1bdm, PDBj:1bdm
PDBsum1bdm
PubMed8471603
UniProtP10584|MDH_THETH Malate dehydrogenase (Gene Name=mdh)

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