1rhy

X-ray diffraction
2.3Å resolution

Crystal structure of Imidazole Glycerol Phosphate Dehydratase

Released:

Function and Biology Details

Reaction catalysed:
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-143545 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazoleglycerol-phosphate dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 22.01 KDa
Source organism: Cryptococcus neoformans
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CO22 (Residues: 1-202; Coverage: 100%)
Gene names: CNH01620, HIS3
Sequence domains: Imidazoleglycerol-phosphate dehydratase
Structure domains: Imidazole glycerol phosphate dehydratase; domain 1

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P213
Unit cell:
a: 105.275Å b: 105.275Å c: 105.275Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.228
Expression system: Escherichia coli