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-139222 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Exocyst complex component SEC3
Molecule details ›
Chains: A, C, E
Length: 320 amino acids
Theoretical weight: 36.27 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Exocyst complex component SEC3 N-terminal PIP2 binding PH
Structure domains: PH-domain like
Length: 320 amino acids
Theoretical weight: 36.27 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P33332 (Residues: 1-320; Coverage: 24%)
Sequence domains: Exocyst complex component SEC3 N-terminal PIP2 binding PH
Structure domains: PH-domain like
GTP-binding protein RHO1
Molecule details ›
Chains: B, D, F
Length: 188 amino acids
Theoretical weight: 20.77 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 188 amino acids
Theoretical weight: 20.77 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: P06780 (Residues: 1-188; Coverage: 90%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
