› 1a9c

X-ray diffraction
2.9Å resolution

GTP CYCLOHYDROLASE I (C110S MUTANT) IN COMPLEX WITH GTP

Released:
DOI: 10.2210/pdb1a9c/pdb
PDB entry 1a9c coloured by chain, front view.
PDB entry 1a9c coloured by chain, side view.
PDB entry 1a9c coloured by chain, top view.
Source organism: Escherichia coli
Entry authors: Auerbach G, Nar H, Bracher A, Bacher A, Huber R

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-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
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 221 amino acids
Theoretical weight: 24.72 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 GTP 15 x GTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 313.9Å b: 226.8Å c: 131.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.288
Expression system: Escherichia coli

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