› 1ide

X-ray diffraction
2.5Å resolution

ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)

Released:
DOI: 10.2210/pdb1ide/pdb
PDB entry 1ide coloured by chain, front view.
PDB entry 1ide coloured by chain, side view.
PDB entry 1ide coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.
Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE, Stoddard BL
Science 268 1312-8 (1995)
PMID: 7761851

Function and Biology Details

Reaction catalysed: 
(1a) isocitrate + NADP(+) = 2-oxalosuccinate + NADPH
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-530542 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 45.79 KDa
Source organism: Escherichia coli
Expression system: PEMBL (DENTE ET AL 1983 NUC ACIDS RES 11,1645)
UniProt:
  • Canonical: P08200 (Residues: 1-416; Coverage: 100%)
Gene names: JW1122, b1136, icd, icdA, icdE
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:
Ligand MG 1 x MG
Ligand ICT 1 x ICT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P43212
Unit cell:
a: 105.1Å b: 105.1Å c: 150.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 not available
Expression system: PEMBL (DENTE ET AL 1983 NUC ACIDS RES 11,1645)

Quick links

Citations

17 review citations

Isocitrate dehydrogenase-1 mutations: a fundamentally new understanding of diffuse glioma?
Kloosterhof et al. (2011)
16 more

2 mentions without citation

The skeletal muscle Ca2+ release channel has an oxidoreductase-like domain.
Baker et al. (2002)
1 more