› 1wur

X-ray diffraction
1.82Å 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
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SH52 (Residues: 1-220; Coverage: 100%)
Gene names: TTHA1878, folE
Sequence domains: GTP cyclohydrolase I
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 5 x ZN
Ligand 8DG 5 x 8DG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: C2
Unit cell:
a: 160.57Å b: 110.56Å c: 70.53Å
α: 90° β: 105.78° γ: 90°
R-values:
R R work R free
0.206 0.206 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Folate biosynthesis pathway: mechanisms and insights into drug design for infectious diseases.
Bertacine Dias et al. (2018)
1 more

5 mentions without citation

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