Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158288 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rho guanine nucleotide exchange factor 12
Molecule details ›
Chains: A, C, E, G
Length: 385 amino acids
Theoretical weight: 44.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 385 amino acids
Theoretical weight: 44.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9NZN5 (Residues: 766-1138; Coverage: 24%)
Sequence domains:
Structure domains:
Transforming protein RhoA
Molecule details ›
Chains: B, D, F, H
Length: 196 amino acids
Theoretical weight: 22.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 196 amino acids
Theoretical weight: 22.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P61586 (Residues: 1-193; Coverage: 100%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
