PDBe 3msx

X-ray diffraction
1.65Å resolution

Crystal structure of RhoA.GDP.MgF3 in complex with GAP domain of ArhGAP20

Released:
Source organism: Homo sapiens
Entry authors: Utepbergenov D, Cooper DR, Derewenda U, Derewenda ZS

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transforming protein RhoA Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 20.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61586 (Residues: 1-180; Coverage: 93%)
Gene names: ARH12, ARHA, RHO12, RHOA
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Rho GTPase-activating protein 20 Chain: B
Molecule details ›
Chain: B
Length: 201 amino acids
Theoretical weight: 22.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P2F6 (Residues: 351-551; Coverage: 17%)
Gene names: ARHGAP20, KIAA1391
Sequence domains: RhoGAP domain
Structure domains: Rho GTPase activation protein

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2221
Unit cell:
a: 69.057Å b: 88.977Å c: 137.725Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.219
Expression system: Escherichia coli