› 1ai3

X-ray diffraction
1.9Å resolution

ORBITAL STEERING IN THE CATALYTIC POWER OF ENZYMES: SMALL STRUCTURAL CHANGES WITH LARGE CATALYTIC CONSEQUENCES

Released:
DOI: 10.2210/pdb1ai3/pdb
PDB entry 1ai3 coloured by chain, front view.
PDB entry 1ai3 coloured by chain, side view.
PDB entry 1ai3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences.
Mesecar AD, Stoddard BL, Koshland DE
Science 277 202-6 (1997)
PMID: 9211842

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: Escherichia coli
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 NDO 1 x NDO
2 bound ligands:
Ligand ICT 1 x ICT
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P43212
Unit cell:
a: 102.4Å b: 102.4Å c: 150.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.22
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Calcineurin: form and function.
Rusnak et al. (2000)
17 more

3 mentions without citation

From the similarity analysis of protein cavities to the functional classification of protein families using cavbase.
Kuhn et al. (2006)
2 more