› 2x2r

X-ray diffraction
2.2Å resolution

Crystal structure of human kinesin Eg5 in complex with (R)-2-amino-3-((4-chlorophenyl)diphenylmethylthio)propanoic acid

Released:
DOI: 10.2210/pdb2x2r/pdb
PDB entry 2x2r coloured by chain, front view.
PDB entry 2x2r coloured by chain, side view.
PDB entry 2x2r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-activity relationship and multidrug resistance study of new S-trityl-L-cysteine derivatives as inhibitors of Eg5.
Kaan HY, Weiss J, Menger D, Ulaganathan V, Tkocz K, Laggner C, Popowycz F, Joseph B, Kozielski F
J Med Chem 54 1576-86 (2011)
PMID: 21344920

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156615 (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 X2O 3 x X2O
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P32
Unit cell:
a: 96.35Å b: 96.35Å c: 124.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.172 0.216
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

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

1 mention without citation

Synthesis, cytotoxic assessment, and molecular docking studies of 2,6-diaryl-substituted pyridine and 3,4- dihydropyrimidine-2(1H)-one scaffolds.
Hosseinzadeh et al. (2020)