› 1osi

X-ray diffraction
3Å resolution

STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE

Released:
DOI: 10.2210/pdb1osi/pdb
PDB entry 1osi coloured by chain, front view.
PDB entry 1osi coloured by chain, side view.
PDB entry 1osi coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase.
Qu C, Akanuma S, Moriyama H, Tanaka N, Oshima T
Protein Eng 10 45-52 (1997)
PMID: 9051733

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-177982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-isopropylmalate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 36.83 KDa
Source organism: Thermus thermophilus HB8
Expression system: unidentified
UniProt:
  • Canonical: Q5SIY4 (Residues: 1-345; Coverage: 100%)
Gene names: TTHA1230, 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
Spacegroup: P21
Unit cell:
a: 82.5Å b: 86.7Å c: 112.1Å
α: 90° β: 90.7° γ: 90°
R-values:
R R work R free
0.149 0.149 not available
Expression system: unidentified

Quick links

Citations

8 citation in other articles

Protein rigidity and thermophilic adaptation.
Radestock et al. (2011)
7 more

2 mentions without citation

Ancestral sequence reconstruction produces thermally stable enzymes with mesophilic enzyme-like catalytic properties.
Furukawa et al. (2020)
1 more