Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158606 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
T3SS secreted effector EspG
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 40.03 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: EspG protein
Structure domains: EspG protein, N-terminal domain
Length: 357 amino acids
Theoretical weight: 40.03 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q7DB50 (Residues: 25-381; Coverage: 94%)
Sequence domains: EspG protein
Structure domains: EspG protein, N-terminal domain
ADP-ribosylation factor 6
Molecule details ›
Chain: B
Length: 162 amino acids
Theoretical weight: 18.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 162 amino acids
Theoretical weight: 18.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P62330 (Residues: 14-175; Coverage: 93%)
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
