› 1idm

X-ray diffraction
2.2Å resolution

3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA

Released:
DOI: 10.2210/pdb1idm/pdb
PDB entry 1idm coloured by chain, front view.
PDB entry 1idm coloured by chain, side view.
PDB entry 1idm coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism.
Sakurai M, Ohzeki M, Miyazaki K, Moriyama H, Sato M, Tanaka N, Oshima T
Acta Crystallogr D Biol Crystallogr 52 124-8 (1996)
PMID: 15299733

Function and Biology Details

Reaction catalysed: 
(1a) (2R,3S)-3-isopropylmalate + NAD(+) = (2S)-2-isopropyl-3-oxosuccinate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
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: 343 amino acids
Theoretical weight: 36.47 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SIY4 (Residues: 1-77, 78-345; Coverage: 99%)
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: 78.45Å b: 78.45Å c: 158.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis.
Singh et al. (2005)
1 more

1 mention without citation

Homology induction: the use of machine learning to improve sequence similarity searches.
Karwath et al. (2002)