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-127285 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rho guanine nucleotide exchange factor 11
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 44.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 383 amino acids
Theoretical weight: 44.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O15085 (Residues: 710-1085; Coverage: 25%)
Sequence domains:
Structure domains:
Transforming protein RhoA
Molecule details ›
Chains: E, F
Length: 182 amino acids
Theoretical weight: 20.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 182 amino acids
Theoretical weight: 20.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P61586 (Residues: 1-181; Coverage: 94%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
