Function and Biology Details
Reactions catalysed:
GTP + H(2)O = GDP + phosphate
ATP + H(2)O + xenobiotic(Side 1) = ADP + phosphate + xenobiotic(Side 2)
ATP + H(2)O + glutathione-S-conjugate(Side 1) = ADP + phosphate + glutathione-S-conjugate(Side 2)
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145724 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Ral-B
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 178 amino acids
Theoretical weight: 20.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P11234 (Residues: 8-185; Coverage: 86%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
RalA-binding protein 1
Molecule details ›
Chain: B
Length: 56 amino acids
Theoretical weight: 6.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: RLIP76, Ral binding domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Length: 56 amino acids
Theoretical weight: 6.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q15311 (Residues: 393-446; Coverage: 8%)
Sequence domains: RLIP76, Ral binding domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
