› 5cit

X-ray diffraction
1.75Å resolution

Ran GDP wild type monoclinic crystal form

Released:
DOI: 10.2210/pdb5cit/pdb
PDB entry 5cit coloured by chain, front view.
PDB entry 5cit coloured by chain, side view.
PDB entry 5cit coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental, and theoretical IR spectroscopy.
Rudack T, Jenrich S, Brucker S, Vetter IR, Gerwert K, Kötting C
J Biol Chem 290 24079-90 (2015)
PMID: 26272610

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158719 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP-binding nuclear protein Ran Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 24.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62826 (Residues: 1-216; Coverage: 100%)
Gene names: ARA24, OK/SW-cl.81, RAN
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand GDP 2 x GDP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 58.01Å b: 59.23Å c: 64.77Å
α: 90° β: 96.95° γ: 90°
R-values:
R R work R free
0.219 0.216 0.262
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Invited review: Small GTPases and their GAPs.
Mishra et al. (2016)
2 more

2 mentions without citation

Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental, and theoretical IR spectroscopy.
Rudack et al. (2015)
1 more