› 3zcw

X-ray diffraction
1.69Å resolution

Eg5 - New allosteric binding site

Released:
DOI: 10.2210/pdb3zcw/pdb
PDB entry 3zcw coloured by chain, front view.
PDB entry 3zcw coloured by chain, side view.
PDB entry 3zcw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into a unique inhibitor binding pocket in kinesin spindle protein.
Ulaganathan V, Talapatra SK, Rath O, Pannifer A, Hackney DD, Kozielski F
J Am Chem Soc 135 2263-72 (2013)
PMID: 23305346

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-156612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinesin-like protein KIF11 Chain: A
Molecule details ›
Chain: A
Length: 348 amino acids
Theoretical weight: 38.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P52732 (Residues: 16-363; Coverage: 33%)
Gene names: EG5, KIF11, KNSL1, TRIP5
Sequence domains: Kinesin motor domain
Structure domains: Kinesin motor domain

Ligands and Environments

5 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
Ligand 4A2 2 x 4A2
Ligand EPE 1 x EPE
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 107.94Å b: 62.89Å c: 75.05Å
α: 90° β: 117.46° γ: 90°
R-values:
R R work R free
0.196 0.194 0.233
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Kinesin-5: cross-bridging mechanism to targeted clinical therapy.
Wojcik et al. (2013)
2 more

11 mentions without citation

Recent findings and future directions for interpolar mitotic kinesin inhibitors in cancer therapy.
Myers et al. (2016)
10 more