1is7

X-ray diffraction
2.8Å resolution

Crystal structure of rat GTPCHI/GFRP stimulatory complex

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:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only icosamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: 230 amino acids
Theoretical weight: 25.82 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P22288 (Residues: 12-241; Coverage: 95%)
Gene names: Gch, Gch1
Sequence domains: GTP cyclohydrolase I
Structure domains:
GTP cyclohydrolase 1 feedback regulatory protein Chains: K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: K, L, M, N, O, P, Q, R, S, T
Length: 84 amino acids
Theoretical weight: 9.68 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P70552 (Residues: 1-84; Coverage: 100%)
Gene names: Gchfr, Gfrp
Sequence domains: GTP cyclohydrolase I feedback regulatory protein (GFRP)
Structure domains: GTP cyclohydrolase I feedback regulatory protein GFRP

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 124.151Å b: 111.723Å c: 126.108Å
α: 90° β: 97.37° γ: 90°
R-values:
R R work R free
0.228 0.228 0.264
Expression system: Escherichia coli