Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156303 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
PNPLA domain-containing protein
Molecule details ›
Chains: A, C, E, G
Length: 551 amino acids
Theoretical weight: 61.23 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli
UniProt:
Sequence domains: Patatin-like phospholipase
Structure domains: Cytosolic phospholipase A2 catalytic domain
Length: 551 amino acids
Theoretical weight: 61.23 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli
UniProt:
- Canonical:
Q5ZRP9 (Residues: 19-564; Coverage: 88%)
Sequence domains: Patatin-like phospholipase
Structure domains: Cytosolic phospholipase A2 catalytic domain
Ras-related protein Rab-5C
Molecule details ›
Chains: B, D, F, H
Length: 170 amino acids
Theoretical weight: 18.79 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: 18.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P51148 (Residues: 18-182; Coverage: 76%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
