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-158279 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Unconventional myosin-IXb
Molecule details ›
Chains: A, D
Length: 232 amino acids
Theoretical weight: 26.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: RhoGAP domain
Structure domains: Rho GTPase activation protein
Length: 232 amino acids
Theoretical weight: 26.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q13459 (Residues: 1691-1916; Coverage: 11%)
Sequence domains: RhoGAP domain
Structure domains: Rho GTPase activation protein
Transforming protein RhoA
Molecule details ›
Chains: B, F
Length: 185 amino acids
Theoretical weight: 20.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 185 amino acids
Theoretical weight: 20.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P61586 (Residues: 3-181; Coverage: 93%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
