› 3icd

X-ray diffraction
2.5Å resolution

STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE

Released:
DOI: 10.2210/pdb3icd/pdb
PDB entry 3icd coloured by chain, front view.
PDB entry 3icd coloured by chain, side view.
PDB entry 3icd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE, Stroud RM
Proc Natl Acad Sci U S A 86 8635-9 (1989)
PMID: 2682654

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-140025 (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: Not provided
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
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
0.18 0.18 not available
Expression system: Not provided

Quick links

Citations

13 review citations

Principles of protein-protein interactions.
Jones et al. (1996)
12 more

5 mentions without citation

Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase.
Dean et al. (1997)
4 more