› 3k3b

X-ray diffraction
2.4Å resolution

Co-crystal structure of the human kinesin Eg5 with a novel tetrahydro-beta-carboline

Released:
DOI: 10.2210/pdb3k3b/pdb
PDB entry 3k3b coloured by chain, front view.
PDB entry 3k3b coloured by chain, side view.
PDB entry 3k3b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The discovery of tetrahydro-beta-carbolines as inhibitors of the kinesin Eg5.
Barsanti PA, Wang W, Ni ZJ, Duhl D, Brammeier N, Martin E, Bussiere D, Walter AO
Bioorg Med Chem Lett 20 157-60 (2010)
PMID: 19945875

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-156612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinesin-like protein KIF11 Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 41.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

6 bound ligands:
Ligand MG 2 x MG
Ligand ADP 2 x ADP
Ligand L31 2 x L31
Ligand NO3 2 x NO3
Ligand CL 1 x CL
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 78.97Å b: 92.67Å c: 102.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.243
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

3 mentions without citation

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