› 5lt1

X-ray diffraction
1.95Å resolution

nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form

Released:
DOI: 10.2210/pdb5lt1/pdb
PDB entry 5lt1 coloured by chain, front view.
PDB entry 5lt1 coloured by chain, side view.
PDB entry 5lt1 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
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
Molecule details ›
Chains: A, B
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

3 bound ligands:
Ligand SO4 3 x SO4
Ligand ACT 4 x ACT
Ligand SR 1 x SR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 53.903Å b: 69.921Å c: 100.139Å
α: 90° β: 100.81° γ: 90°
R-values:
R R work R free
0.196 0.194 0.236
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

1 mention without citation

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