PDBe 3hqd

X-ray diffraction
2.19Å resolution

Human kinesin Eg5 motor domain in complex with AMPPNP and Mg2+

Released:
Source organism: Homo sapiens
Primary publication:
ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism.
J. Biol. Chem. 285 5859-67 (2010)
PMID: 20018897

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinesin-like protein KIF11 Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 41.17 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

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 60.5Å b: 71.435Å c: 94.846Å
α: 90° β: 98.86° γ: 90°
R-values:
R R work R free
0.224 0.224 0.262
Expression system: Escherichia coli