PDBe 1cc0

X-ray diffraction
5Å resolution

CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX

Released:
Source organism: Homo sapiens
Primary publication:
How RhoGDI binds Rho.
Acta Crystallogr. D Biol. Crystallogr. 55 1503-15 (1999)
PMID: 10489445

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transforming protein RhoA Chains: A, C
Molecule details ›
Chains: A, C
Length: 190 amino acids
Theoretical weight: 21.44 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61586 (Residues: 1-190; Coverage: 98%)
Gene names: ARH12, ARHA, RHO12, RHOA
Sequence domains: Ras family
Rho GDP-dissociation inhibitor 1 Chains: E, F
Molecule details ›
Chains: E, F
Length: 204 amino acids
Theoretical weight: 23.24 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P52565 (Residues: 1-204; Coverage: 100%)
Gene names: ARHGDIA, GDIA1
Sequence domains: RHO protein GDP dissociation inhibitor

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6522
Unit cell:
a: 139.3Å b: 139.3Å c: 253.1Å
α: 90° β: 90° γ: 120°
Expression system: Saccharomyces cerevisiae