Function and Biology Details
Reactions catalysed:
GTP + H(2)O = GDP + phosphate
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
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-133972 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase HRas, N-terminally processed
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 19.38 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: 173 amino acids
Theoretical weight: 19.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P01112 (Residues: 1-166; Coverage: 88%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
Molecule details ›
Chains: C, D
Length: 117 amino acids
Theoretical weight: 13.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Ras association (RalGDS/AF-6) domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 117 amino acids
Theoretical weight: 13.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q9P212 (Residues: 2131-2246; Coverage: 5%)
Sequence domains: Ras association (RalGDS/AF-6) domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
