› 1idc

X-ray diffraction
2.5Å resolution

ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY

Released:
DOI: 10.2210/pdb1idc/pdb
PDB 1idc coloured by chain and viewed from the front.
PDB 1idc coloured by chain and viewed from the side.
PDB 1idc coloured by chain and viewed from the top.
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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 45.81 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

2 bound ligands:
Ligand MG 1 x MG
Ligand OXS 1 x OXS
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
0.169 0.169 not available
Expression system: PEMBL (DENTE ET AL 1983 NUC ACIDS RES 11,1645)

Quick links

Citations

15 review citations

Serial femtosecond crystallography: A revolution in structural biology.
Martin-Garcia et al. (2016)
14 more

1 mention without citation

Induced fit and the catalytic mechanism of isocitrate dehydrogenase.
Gonçalves et al. (2012)