Research workbench
Structural basis for the assembly of the mitotic motor kinesin-5 into bipolar tetramers
Analyse Structural basis for the assembly of the mitotic motor kinesin-5 into bipolar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PXU
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.601
- Source
- Drosophila melanogaster
- Molecule
- Bipolar kinesin KRP-130
- UniProt
- P46863
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · resolution 2.601 · 2 distinct chains · 94% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bipolar kinesin KRP-130 | protein | 152 | 97% helix, 0% strand | P46863 |
| B | Bipolar kinesin KRP-130 | protein | 136 | 90% helix, 0% strand | P46863 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.42 | 0.81 | 16 | empty |
| 2 | 59 | 0.42 | 0.82 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2727 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4PXU · Structural basis for the assembly of the mitotic motor kinesin-5 into bipolar tetramers · the same entry in another collection · chain A against A, TM-score 1.00
- P46863 · AlphaFold monomer V2.0 prediction for kinesin-like protein KLP61F (P46863) · a predicted model of the same protein · chain B against A, TM-score 0.75
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P46863
- Elsewhere: RCSB PDB 4PXU · PDBe 4PXU · UniProt P46863
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