2f1d

X-ray diffraction
3Å resolution

X-Ray Structure of imidazoleglycerol-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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo 24-mer
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazoleglycerol-phosphate dehydratase 1, chloroplastic Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 207 amino acids
Theoretical weight: 22.41 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P34047 (Residues: 64-270; Coverage: 77%)
Gene names: At3g22425, HISN5A, MCB17.17
Sequence domains: Imidazoleglycerol-phosphate dehydratase
Structure domains: Imidazole glycerol phosphate dehydratase; domain 1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R3
Unit cell:
a: 157.949Å b: 157.949Å c: 479.965Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.243 0.24 0.286
Expression system: Escherichia coli BL21(DE3)