› 1fso

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI QUADRUPLE MUTANT

Released:
DOI: 10.2210/pdb1fso/pdb
PDB entry 1fso coloured by chain, front view.
PDB entry 1fso coloured by chain, side view.
PDB entry 1fso coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI.
Longenecker KL, Garrard SM, Sheffield PJ, Derewenda ZS
Acta Crystallogr D Biol Crystallogr 57 679-88 (2001)
PMID: 11320308

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156565 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rho GDP-dissociation inhibitor 1 Chain: A
Molecule details ›
Chain: A
Length: 139 amino acids
Theoretical weight: 15.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52565 (Residues: 67-204; Coverage: 68%)
Gene names: ARHGDIA, GDIA1
Sequence domains: RHO protein GDP dissociation inhibitor
Structure domains: Coagulation Factor XIII, subunit A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P3221
Unit cell:
a: 76.29Å b: 76.29Å c: 88.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.217 0.232
Expression system: Escherichia coli

Quick links

Citations

8 review citations

High-throughput crystallography for lead discovery in drug design.
Blundell et al. (2002)
7 more

3 mentions without citation

The regulatory subunit ε in Escherichia coli FOF1-ATP synthase.
Sielaff et al. (2018)
2 more