Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Ras guanine-nucleotide exchange factors catalytic domain
- Ras-like guanine nucleotide exchange factor, N-terminal
- Small GTPase
- P-loop containing nucleoside triphosphate hydrolase
- Ras guanine-nucleotide exchange factor, conserved site
- Ras guanine-nucleotide exchange factor, catalytic domain superfamily
- Ras-like guanine nucleotide exchange factor
- Ras guanine nucleotide exchange factor domain superfamily
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134021 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase KRas, N-terminally processed
Molecule details ›
Chain: R
Length: 170 amino acids
Theoretical weight: 19.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 170 amino acids
Theoretical weight: 19.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P01116 (Residues: 1-169; Coverage: 89%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Son of sevenless homolog 1
Molecule details ›
Chain: S
Length: 487 amino acids
Theoretical weight: 57.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 487 amino acids
Theoretical weight: 57.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q07889 (Residues: 563-1049; Coverage: 37%)
Sequence domains:
Structure domains:
