› 3wpn

X-ray diffraction
2.8Å resolution

Kinesin spindle protein Eg5 in complex with ATP-competitive inhibitor PVZB1194

Released:
DOI: 10.2210/pdb3wpn/pdb
PDB entry 3wpn coloured by chain, front view.
PDB entry 3wpn coloured by chain, side view.
PDB entry 3wpn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of new allosteric inhibition in Kinesin spindle protein Eg5.
Yokoyama H, Sawada J, Katoh S, Matsuno K, Ogo N, Ishikawa Y, Hashimoto H, Fujii S, Asai A
ACS Chem Biol 10 1128-36 (2015)
PMID: 25622007

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: 382 amino acids
Theoretical weight: 42.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52732 (Residues: 1-369; Coverage: 35%)
Gene names: EG5, KIF11, KNSL1, TRIP5
Sequence domains: Kinesin motor domain
Structure domains: Kinesin motor domain

Ligands and Environments

1 bound ligand:
Ligand B4S 1 x B4S
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 71.912Å b: 95.425Å c: 59.015Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.225 0.29
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Kinesin, 30 years later: Recent insights from structural studies.
Wang et al. (2015)
1 more

4 mentions without citation

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