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-158147 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cell division control protein 42 homolog
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 20.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 182 amino acids
Theoretical weight: 20.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P60953 (Residues: 2-178; Coverage: 93%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Chaperone (IpgB2)
Molecule details ›
Chain: B
Length: 172 amino acids
Theoretical weight: 19.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: IpaB/EvcA family
Structure domains: SopE-like GEF fold
Length: 172 amino acids
Theoretical weight: 19.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: Q9R8E4 (Residues: 37-203; Coverage: 82%)
Sequence domains: IpaB/EvcA family
Structure domains: SopE-like GEF fold
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007
Spacegroup:
P212121
Expression system: Escherichia coli
