› 1n3s

X-ray diffraction
2.55Å resolution

Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I

Released:
DOI: 10.2210/pdb1n3s/pdb
PDB entry 1n3s coloured by chain, front view.
PDB entry 1n3s coloured by chain, side view.
PDB entry 1n3s coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.
Rebelo J, Auerbach G, Bader G, Bracher A, Nar H, Hösl C, Schramek N, Kaiser J, Bacher A, Huber R, Fischer M
J Mol Biol 326 503-16 (2003)
PMID: 12559918

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

Assemblies composition:
homo pentamer (preferred)
homo decamer
Assembly name:
PDBe Complex ID:
PDB-CPX-141425 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP cyclohydrolase 1 Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 221 amino acids
Theoretical weight: 24.68 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 10 x GTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P43212
Unit cell:
a: 124.302Å b: 124.302Å c: 389.125Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.282 0.262 0.293
Expression system: Escherichia coli

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Citations

6 review citations

On the origin of biochemistry at an alkaline hydrothermal vent.
Martin et al. (2007)
5 more