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 domains:
Structure analysis Details
Assembly composition:
hetero icosamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149569 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTP cyclohydrolase 1
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:
Sequence domains: GTP cyclohydrolase I
Structure domains:
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%)
Sequence domains: GTP cyclohydrolase I
Structure domains:
GTP cyclohydrolase 1 feedback regulatory protein
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:
Sequence domains: GTP cyclohydrolase I feedback regulatory protein (GFRP)
Structure domains: GTP cyclohydrolase I feedback regulatory protein GFRP
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%)
Sequence domains: GTP cyclohydrolase I feedback regulatory protein (GFRP)
Structure domains: GTP cyclohydrolase I feedback regulatory protein GFRP
