› 2ayq

X-ray diffraction
3Å resolution

3-ISOPROPYLMALATE DEHYDROGENASE FROM THE MODERATE FACULTATIVE THERMOPHILE, BACILLUS COAGULANS

Released:
DOI: 10.2210/pdb2ayq/pdb
PDB entry 2ayq coloured by chain, front view.
PDB entry 2ayq coloured by chain, side view.
PDB entry 2ayq coloured by chain, top view.
Source organism: Weizmannia coagulans
Primary publication:
Crystal structure of 3-isopropylmalate dehydrogenase from the moderate facultative thermophile, Bacillus coagulans: two strategies for thermostabilization of protein structures.
Tsuchiya D, Sekiguchi T, Takenaka A
J Biochem 122 1092-104 (1997)
PMID: 9498551

Function and Biology Details

Reaction catalysed: 
(1a) (2R,3S)-3-isopropylmalate + NAD(+) = (2S)-2-isopropyl-3-oxosuccinate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-isopropylmalate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 39.86 KDa
Source organism: Weizmannia coagulans
Expression system: Escherichia coli
UniProt:
  • Canonical: P12010 (Residues: 1-366; Coverage: 100%)
Gene name: leuB
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P3121
Unit cell:
a: 114.4Å b: 114.4Å c: 194.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.247
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.
Amorim Franco et al. (2017)
9 other articles