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-160801 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ADP-ribosylation factor 1
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 166 amino acids
Theoretical weight: 18.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P84078 (Residues: 18-181; Coverage: 91%)
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
ADP-ribosylation factor-binding protein GGA1
Molecule details ›
Chain: B
Length: 45 amino acids
Theoretical weight: 5.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: N-terminal extension of GAT domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 45 amino acids
Theoretical weight: 5.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q9UJY5 (Residues: 166-210; Coverage: 7%)
Sequence domains: N-terminal extension of GAT domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
