› 1fb1

X-ray diffraction
3.1Å resolution

CRYSTAL STRUCTURE OF HUMAN GTP CYCLOHYDROLASE I

Released:
DOI: 10.2210/pdb1fb1/pdb
PDB entry 1fb1 coloured by chain, front view.
PDB entry 1fb1 coloured by chain, side view.
PDB entry 1fb1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Zinc plays a key role in human and bacterial GTP cyclohydrolase I.
Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A
Proc Natl Acad Sci U S A 97 13567-72 (2000)
PMID: 11087827

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

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
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:
Ligand ZN 5 x ZN
Ligand IPA 5 x IPA
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

Quick links

Citations

14 review citations

Tetrahydrobiopterin: biochemistry and pathophysiology.
Werner et al. (2011)
13 more

13 mentions without citation

Zinc-binding cysteines: diverse functions and structural motifs.
Pace et al. (2014)
12 more