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-related protein Rap1
- Small GTPase, Ras-type
- Small GTP-binding protein domain
- Ras guanine-nucleotide exchange factor, catalytic domain superfamily
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158237 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RAS guanyl-releasing protein 2
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 397 amino acids
Theoretical weight: 45.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 397 amino acids
Theoretical weight: 45.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q7LDG7 (Residues: 1-394; Coverage: 65%)
Sequence domains:
Ras-related protein Rap-1b
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 169 amino acids
Theoretical weight: 19.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 169 amino acids
Theoretical weight: 19.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P61224 (Residues: 1-167; Coverage: 91%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
