Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158281 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Guanine nucleotide exchange factor DBS
Molecule details ›
Chains: A, C, E, G
Length: 353 amino acids
Theoretical weight: 41.25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 353 amino acids
Theoretical weight: 41.25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q64096 (Residues: 623-967; Coverage: 30%)
Sequence domains:
Structure domains:
Transforming protein RhoA
Molecule details ›
Chains: B, D, F, H
Length: 192 amino acids
Theoretical weight: 21.59 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: 192 amino acids
Theoretical weight: 21.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P61586 (Residues: 1-190; Coverage: 98%)
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 19-BM
Spacegroup:
P43
Expression system: Escherichia coli BL21(DE3)
