Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145722 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Ral-A
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 23.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 206 amino acids
Theoretical weight: 23.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P11233 (Residues: 1-206; Coverage: 100%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Mono-ADP-ribosyltransferase C3
Molecule details ›
Chain: B
Length: 251 amino acids
Theoretical weight: 27.88 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: ADP-ribosyltransferase exoenzyme
Structure domains: Toxin ADP-ribosyltransferase; Chain A, domain 1
Length: 251 amino acids
Theoretical weight: 27.88 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical: P15879 (Residues: 1-251; Coverage: 100%)
Sequence domains: ADP-ribosyltransferase exoenzyme
Structure domains: Toxin ADP-ribosyltransferase; Chain A, domain 1
