› 1xad

X-ray diffraction
2.1Å resolution

CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (150K) STRUCTURE.

Released:
DOI: 10.2210/pdb1xad/pdb
PDB entry 1xad coloured by chain, front view.
PDB entry 1xad coloured by chain, side view.
PDB entry 1xad coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme.
Nagata C, Moriyama H, Tanaka N, Nakasako M, Yamamoto M, Ueki T, Oshima T
Acta Crystallogr D Biol Crystallogr 52 623-30 (1996)
PMID: 15299625

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 Chain: A
Molecule details ›
Chain: A
Length: 345 amino acids
Theoretical weight: 37.06 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: P3221
Unit cell:
a: 77.4Å b: 77.4Å c: 156.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 not available
Expression system: unidentified

Quick links

Citations

1 review citation

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