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-133966 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ral guanine nucleotide dissociation stimulator
Molecule details ›
Chains: A, C
Length: 87 amino acids
Theoretical weight: 9.99 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras association (RalGDS/AF-6) domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 87 amino acids
Theoretical weight: 9.99 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q03386 (Residues: 778-864; Coverage: 10%)
Sequence domains: Ras association (RalGDS/AF-6) domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
GTPase HRas, N-terminally processed
Molecule details ›
Chains: B, D
Length: 167 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 167 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P01112 (Residues: 1-167; Coverage: 88%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
