› 1pb3

X-ray diffraction
1.7Å resolution

Sites of binding and orientation in a four location model for protein stereospecificity.

Released:
DOI: 10.2210/pdb1pb3/pdb
PDB entry 1pb3 coloured by chain, front view.
PDB entry 1pb3 coloured by chain, side view.
PDB entry 1pb3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Sites of binding and orientation in a four-location model for protein stereospecificity.
Mesecar AD, Koshland DE
IUBMB Life 49 457-66 (2000)
PMID: 10902579

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

2 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P43212
Unit cell:
a: 103.669Å b: 103.669Å c: 150.124Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.216
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Human D-Amino Acid Oxidase: Structure, Function, and Regulation.
Pollegioni et al. (2018)
2 more

1 mention without citation

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