Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129930 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ADP-ribosylation factor 6
Molecule details ›
Chains: A, B, E
Length: 165 amino acids
Theoretical weight: 18.99 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: 165 amino acids
Theoretical weight: 18.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62330 (Residues: 13-175; Coverage: 93%)
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
C-Jun-amino-terminal kinase-interacting protein 4
Molecule details ›
Chains: C, D
Length: 77 amino acids
Theoretical weight: 8.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: JNK-interacting protein leucine zipper II
Structure domains: arf6 gtpase in complex with a specific effector, jip4
Length: 77 amino acids
Theoretical weight: 8.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: O60271 (Residues: 406-476; Coverage: 5%)
Sequence domains: JNK-interacting protein leucine zipper II
Structure domains: arf6 gtpase in complex with a specific effector, jip4
