Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Guanine nucleotide binding protein (G-protein), alpha subunit
- RGS domain
- G-protein alpha subunit, group Q
- G protein alpha subunit, helical insertion
- P-loop containing nucleoside triphosphate hydrolase
- RGS, subdomain 2
- Regulator of G-protein signalling 2, regulator of G protein signaling domain
- RGS, subdomain 1/3
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149198 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Guanine nucleotide-binding protein G(q) subunit alpha
Molecule details ›
Chain: A
Length: 347 amino acids
Theoretical weight: 40.63 KDa
Source organism: Mus musculus
Expression system: Trichoplusia ni
UniProt:
Sequence domains: G-protein alpha subunit
Structure domains:
Length: 347 amino acids
Theoretical weight: 40.63 KDa
Source organism: Mus musculus
Expression system: Trichoplusia ni
UniProt:
- Canonical:
P21279 (Residues: 18-359; Coverage: 95%)
Sequence domains: G-protein alpha subunit
Structure domains:
Regulator of G-protein signaling 2
Molecule details ›
Chain: B
Length: 137 amino acids
Theoretical weight: 15.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Regulator of G protein signaling domain
Structure domains:
Length: 137 amino acids
Theoretical weight: 15.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P41220 (Residues: 72-203; Coverage: 63%)
Sequence domains: Regulator of G protein signaling domain
Structure domains:
