› 1dpz

X-ray diffraction
2.8Å resolution

STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711

Released:
DOI: 10.2210/pdb1dpz/pdb
PDB entry 1dpz coloured by chain, front view.
PDB entry 1dpz coloured by chain, side view.
PDB entry 1dpz coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
Nurachman Z, Akanuma S, Sato T, Oshima T, Tanaka N
Protein Eng 13 253-8 (2000)
PMID: 10810156

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
Molecule details ›
Chains: A, B
Length: 349 amino acids
Theoretical weight: 37.16 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SIY4 (Residues: 1-340; 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
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 55.43Å b: 87.57Å c: 70.89Å
α: 90° β: 100.5° γ: 90°
R-values:
R R work R free
0.177 0.177 0.267
Expression system: Escherichia coli BL21(DE3)

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Citations

4 citation in other articles

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