› 1gtp

X-ray diffraction
3Å resolution

GTP CYCLOHYDROLASE I

Released:
DOI: 10.2210/pdb1gtp/pdb
PDB entry 1gtp coloured by chain, front view.
PDB entry 1gtp coloured by chain, side view.
PDB entry 1gtp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Atomic structure of GTP cyclohydrolase I.
Nar H, Huber R, Meining W, Schmid C, Weinkauf S, Bacher A
Structure 3 459-66 (1995)
PMID: 7663943

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo decamer (preferred)
homo icosamer
Assembly name:
PDBe Complex ID:
PDB-CPX-141423 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP cyclohydrolase 1 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Length: 221 amino acids
Theoretical weight: 24.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6T5 (Residues: 2-222; Coverage: 100%)
Gene names: JW2140, b2153, folE
Sequence domains: GTP cyclohydrolase I
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 20 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 204.2Å b: 210.4Å c: 71.8Å
α: 90° β: 95.8° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Tetrahydrobiopterin biosynthesis, regeneration and functions.
Thöny et al. (2000)
15 more

6 mentions without citation

Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP.
Maita et al. (2002)
5 more