2bz1

X-ray diffraction
1.54Å resolution

CRYSTAL STRUCTURE OF APO E. COLI GTP CYCLOHYDROLASE II

Released:
Source organism: Escherichia coli
Primary publication:
GTP cyclohydrolase II structure and mechanism.
J Biol Chem 280 36912-9 (2005)
PMID: 16115872

Function and Biology Details

Reaction catalysed:
GTP + 4 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP cyclohydrolase-2 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.05 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A7I7 (Residues: 1-196; Coverage: 100%)
Gene names: JW1269, b1277, ribA
Sequence domains: GTP cyclohydrolase II
Structure domains: GTP cyclohydrolase II

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P6522
Unit cell:
a: 71.92Å b: 71.92Å c: 128.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.212
Expression system: Escherichia coli BL21(DE3)