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-158284 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transforming protein RhoA
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 20.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 179 amino acids
Theoretical weight: 20.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P61586 (Residues: 1-179; Coverage: 93%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
ADP ribosyltransferase domain-containing protein
Molecule details ›
Chain: B
Length: 219 amino acids
Theoretical weight: 25.29 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli str. K-12 substr. DH10B
UniProt:
Sequence domains: ADP-ribosyltransferase exoenzyme
Structure domains: Toxin ADP-ribosyltransferase; Chain A, domain 1
Length: 219 amino acids
Theoretical weight: 25.29 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli str. K-12 substr. DH10B
UniProt:
- Canonical: Q8KNY0 (Residues: 1-219; Coverage: 100%)
Sequence domains: ADP-ribosyltransferase exoenzyme
Structure domains: Toxin ADP-ribosyltransferase; Chain A, domain 1
