› 1wm9

X-ray diffraction
2.2Å resolution

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

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177845 (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: 220 amino acids
Theoretical weight: 24.57 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SH52 (Residues: 1-220; Coverage: 100%)
Gene names: TTHA1878, folE
Sequence domains: GTP cyclohydrolase I
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 5 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45PX
Spacegroup: C2
Unit cell:
a: 160.22Å b: 110.477Å c: 70.65Å
α: 90° β: 105.27° γ: 90°
R-values:
R R work R free
0.213 0.208 0.261
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Utility of the Biosynthetic Folate Pathway for Targets in Antimicrobial Discovery.
Bourne CR. (2014)
2 more

3 mentions without citation

Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB.
Sankaran et al. (2009)
2 more