Function and Biology Details
Reactions catalysed:
GTP + H(2)O = GDP + phosphate
GTP + [protein]-L-tyrosine = diphosphate + [protein]-O(4)-(5'-guanylyl)-L-tyrosine
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178600 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ras-related protein Rab-1B
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 19.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 175 amino acids
Theoretical weight: 19.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9H0U4 (Residues: 3-174; Coverage: 86%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Multifunctional virulence effector protein DrrA
Molecule details ›
Chain: B
Length: 197 amino acids
Theoretical weight: 22.01 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: SidM, Rab1-activation domain
Structure domains: Ferritin
Length: 197 amino acids
Theoretical weight: 22.01 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q5ZSQ3 (Residues: 340-533; Coverage: 30%)
Sequence domains: SidM, Rab1-activation domain
Structure domains: Ferritin
