PDBe 1fbx

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF ZINC-CONTAINING E.COLI 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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo decamer (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
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 227.69Å b: 314.19Å c: 132.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.251
Expression system: Escherichia coli