Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-145651 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein BCH1
Molecule details ›
Chains: B, E, H, K
Length: 739 amino acids
Theoretical weight: 83.97 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: ChAPs (Chs5p-Arf1p-binding proteins)
Length: 739 amino acids
Theoretical weight: 83.97 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
Q05029 (Residues: 1-724; Coverage: 100%)
Sequence domains: ChAPs (Chs5p-Arf1p-binding proteins)
ADP-ribosylation factor 1
Molecule details ›
Chains: C, F, I, L
Length: 175 amino acids
Theoretical weight: 19.88 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 175 amino acids
Theoretical weight: 19.88 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical: P11076 (Residues: 18-181; Coverage: 91%)
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
