› 1t5c

X-ray diffraction
2.5Å resolution

Crystal structure of the motor domain of human kinetochore protein CENP-E

Released:
DOI: 10.2210/pdb1t5c/pdb
PDB entry 1t5c coloured by chain, front view.
PDB entry 1t5c coloured by chain, side view.
PDB entry 1t5c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the motor domain of the human kinetochore protein CENP-E.
Garcia-Saez I, Yen T, Wade RH, Kozielski F
J Mol Biol 340 1107-16 (2004)
PMID: 15236970

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Centromere-associated protein E Chains: A, B
Molecule details ›
Chains: A, B
Length: 349 amino acids
Theoretical weight: 39.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02224 (Residues: 2-342; Coverage: 13%)
Gene name: CENPE
Sequence domains: Kinesin motor domain
Structure domains: Kinesin motor domain

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand NO3 1 x NO3
Ligand ADP 2 x ADP
Ligand PIN 1 x PIN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 49.353Å b: 83.7Å c: 94.162Å
α: 90° β: 103.05° γ: 90°
R-values:
R R work R free
0.228 0.228 0.278
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Kinesins and cancer.
Rath et al. (2012)
5 more

9 mentions without citation

Kinesin-2 motors: Kinetics and biophysics.
Gilbert et al. (2018)
8 more