EC Number   |
Subunits |
Reference |
|---|
   5.6.1.3 | ? |
x * 49500, calculated for truncated NcKin3 |
685207 |
| 5.6.1.3 | dimer |
- |
210552, 210553, 210554, 210555, 210556, 669173, 696326 |
| 5.6.1.3 | dimer |
2 * 131000, calculated, full-length protein. 2 * 68000, calculated, truncated protein Kif3-592 |
686499 |
| 5.6.1.3 | dimer |
2 * 248000, Ddunc104, SDS-PAGE |
210553 |
| 5.6.1.3 | dimer |
KIF3A + KIF3B |
210547 |
| 5.6.1.3 | dimer |
Kinesin-1 dimerizes via an extended stalk domain that forms a coiled coil, so that the two catalytic motor domains are situated at one end of the coiled-coil, while cargo-binding domains are found at the opposite end. During active motility, the dimerized motor domains take alternating, eight nanometer steps toward the microtubule plus end, tracking along single protofilaments, structure overview |
733716 |
| 5.6.1.3 | dimer |
molecular dynamics simulation and atomic details of the structural dynamics and energetics of three major ATPase states (ADP, APO, and ATP state) of a human kinesin-1 monomer in complex with a tubulin dimer |
733362 |
| 5.6.1.3 | dimer |
NcKin3 is dimeric but inactivates one of its motor heads to generate nonprocessive motility. The heads of the wild-type Nckin3 motor are strictly coupled via the neck domain, and the dimeric structure is required for proper detachment after one ATPase cycle |
711973 |
| 5.6.1.3 | dimer |
SDS-PAGE |
210552 |
| 5.6.1.3 | heterodimer |
- |
701009 |
