› 2wog

X-ray diffraction
2Å resolution

Intermediate and final states of human kinesin Eg5 in complex with S-trityl-L-cysteine

Released:
DOI: 10.2210/pdb2wog/pdb
PDB entry 2wog coloured by chain, front view.
PDB entry 2wog coloured by chain, side view.
PDB entry 2wog coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An allosteric transition trapped in an intermediate state of a new kinesin-inhibitor complex.
Kaan HY, Ulaganathan V, Hackney DD, Kozielski F
Biochem J 425 55-60 (2009)
PMID: 19793049

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 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 368 amino acids
Theoretical weight: 41.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P52732 (Residues: 1-368; Coverage: 35%)
Gene names: EG5, KIF11, KNSL1, TRIP5
Sequence domains: Kinesin motor domain
Structure domains: Kinesin motor domain

Ligands and Environments

3 bound ligands:
Ligand ADP 3 x ADP
Ligand MG 3 x MG
Ligand ZZD 3 x ZZD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P32
Unit cell:
a: 96.5Å b: 96.5Å c: 124.441Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.155 0.218
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

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

10 mentions without citation

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