PDBe 1fb1

X-ray diffraction
3.1Å resolution

CRYSTAL STRUCTURE OF HUMAN GTP CYCLOHYDROLASE I

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP cyclohydrolase 1 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 196 amino acids
Theoretical weight: 22.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30793 (Residues: 55-250; Coverage: 78%)
Gene names: DYT5, GCH, GCH1
Sequence domains: GTP cyclohydrolase I
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P6522
Unit cell:
a: 115.11Å b: 115.11Å c: 387.31Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.293
Expression system: Escherichia coli