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-158140 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 43.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: RhoGEF domain
Structure domains:
Length: 374 amino acids
Theoretical weight: 43.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q8TCU6 (Residues: 38-408; Coverage: 22%)
Sequence domains: RhoGEF domain
Structure domains:
Cell division control protein 42 homolog
Molecule details ›
Chain: B
Length: 194 amino acids
Theoretical weight: 21.62 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: 194 amino acids
Theoretical weight: 21.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P60953 (Residues: 1-191; Coverage: 100%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 21-ID-D
Spacegroup:
C2221
Expression system: Escherichia coli BL21(DE3)
