6z88

X-ray diffraction
2.69Å resolution

human GTP cyclohydrolase I in complex with allosteric inhibitor

Released:

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP cyclohydrolase 1 Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 224 amino acids
Theoretical weight: 25.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30793 (Residues: 41-250; Coverage: 84%)
Gene names: DYT5, GCH, GCH1
Sequence domains: GTP cyclohydrolase I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 112.355Å b: 161.505Å c: 271.642Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.217 0.254
Expression system: Escherichia coli BL21(DE3)