Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155598 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ADP-ribosylation factor 1
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 164 amino acids
Theoretical weight: 18.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P84077 (Residues: 18-181; Coverage: 91%)
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
ARF guanine-nucleotide exchange factor 1
Molecule details ›
Chain: B
Length: 221 amino acids
Theoretical weight: 25.42 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Sec7 domain
Structure domains:
Length: 221 amino acids
Theoretical weight: 25.42 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: P47102 (Residues: 540-754; Coverage: 15%)
Sequence domains: Sec7 domain
Structure domains:
