› 1kmt

X-ray diffraction
1.3Å resolution

Crystal structure of RhoGDI Glu(154,155)Ala mutant

Released:
DOI: 10.2210/pdb1kmt/pdb
PDB entry 1kmt coloured by chain, front view.
PDB entry 1kmt coloured by chain, side view.
PDB entry 1kmt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The impact of Glu-->Ala and Glu-->Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution.
Mateja A, Devedjiev Y, Krowarsch D, Longenecker K, Dauter Z, Otlewski J, Derewenda ZS
Acta Crystallogr D Biol Crystallogr 58 1983-91 (2002)
PMID: 12454455

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 141 amino acids
Theoretical weight: 15.98 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: P1
Unit cell:
a: 34.099Å b: 35.921Å c: 67.506Å
α: 79.19° β: 82.66° γ: 76.42°
R-values:
R R work R free
0.16 0.158 0.195
Expression system: Escherichia coli

Quick links

Citations

7 review citations

A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.
Moon et al. (2010)
6 more

5 mentions without citation

The role of flexibility and molecular shape in the crystallization of proteins by surface mutagenesis.
Devedjiev YD. (2015)
4 more