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Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.ALFX state, based on cryo-electron microscopy experiment.

Analyse Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CK6
Type
protein
Length
1,199 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tubulin alpha-1D chain; Tubulin beta-2B chain; Kinesin-like protein KIF11
UniProt
Q2HJ86, Q6B856, P52732
Ligands
GTP, GDP, TA1, AF3, ADP, MG
Pockets
1 · best druggability 0.29

Structure

electron microscopy · 3 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulin alpha-1D chainprotein4120% helix, 0% strandQ2HJ86
BTubulin beta-2B chainprotein4260% helix, 0% strandQ6B856
CKinesin-like protein KIF11protein3610% helix, 0% strandP52732

Ligands and binding sites

  • GTP · Guanosine-5'-triphosphate · ligand · chains A
  • GDP · Guanosine-5'-diphosphate · ligand · chains B
  • TA1 · Taxol · ligand · chains B
  • AF3 · Aluminum fluoride · ligand · chains C
  • ADP · Adenosine-5'-diphosphate · ligand · chains C
  • MG · Magnesium ion · metal · 2 copies

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1590.290.7219empty

Interfaces

2 interfaces between chains.

  • A–B · 67 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 62 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4CK6 · Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx… · the same entry in another collection · chain A against A, TM-score 1.00

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