› 5lt4

X-ray diffraction
2.88Å resolution

nucleotide-free kinesin-1 motor domain T92V mutant, P1 crystal form

Released:
DOI: 10.2210/pdb5lt4/pdb
PDB entry 5lt4 coloured by chain, front view.
PDB entry 5lt4 coloured by chain, side view.
PDB entry 5lt4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural switch of nucleotide-free kinesin.
Cao L, Cantos-Fernandes S, Gigant B
OpenAccess logo Sci Rep 7 42558 (2017)
PMID: 28195215

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-152549 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kinesin-1 heavy chain Chains: A, B, C, D, E, K
Molecule details ›
Chains: A, B, C, D, E, K
Length: 325 amino acids
Theoretical weight: 36.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P33176 (Residues: 1-325; Coverage: 34%)
Gene names: KIF5B, KNS, KNS1
Sequence domains: Kinesin motor domain
Structure domains: Kinesin motor domain

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P1
Unit cell:
a: 57.145Å b: 102.108Å c: 102.137Å
α: 119.49° β: 91.95° γ: 91.85°
R-values:
R R work R free
0.208 0.205 0.28
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.
Qin et al. (2020)
1 more

3 mentions without citation

The structural switch of nucleotide-free kinesin.
Cao et al. (2017)
2 more