5c2k

X-ray diffraction
1.42Å resolution

Crystal structure of the fusion protein linked by RhoA and the GAP domain of MgcRacGAP

Released:
Source organism: Homo sapiens
Entry authors: Murayama K, Kato-Murayama M, Hosaka T, Kitamura T, Yokoyama S, Shirouzu M

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rac GTPase-activating protein 1; Transforming protein RhoA Chain: A
Molecule details ›
Chain: A
Length: 415 amino acids
Theoretical weight: 46.07 KDa
Source organism: Homo sapiens
Expression system: Cell-free synthesis
UniProt:
  • Canonical: Q9H0H5 (Residues: 346-546; Coverage: 32%)
  • Canonical: P61586 (Residues: 1-193; Coverage: 100%)
Gene names: ARH12, ARHA, KIAA1478, MGCRACGAP, RACGAP1, RHO12, RHOA
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: P21
Unit cell:
a: 44.491Å b: 77.041Å c: 62.253Å
α: 90° β: 108.53° γ: 90°
R-values:
R R work R free
0.184 0.184 0.206
Expression system: Cell-free synthesis