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The tpr domain of human kinesin light chain 2 (HKLC2)

Analyse The tpr domain of human kinesin light chain 2 (HKLC2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CEQ
Type
protein
Length
519 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin light chain 2
UniProt
Q9H0B6
Pockets
6 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin light chain 2protein25074% helix, 0% strandQ9H0B6
BKinesin light chain 2protein26974% helix, 0% strandQ9H0B6

Pockets

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.570.8128empty
21030.490.8121empty
3690.410.8013empty
4870.400.7815empty
5960.360.7517empty

Interfaces

1 interface between chains.

  • A–B · 1445 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3CEQ · The TPR domain of Human Kinesin Light Chain 2 (hKLC2) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H0B6 · AlphaFold monomer V2.0 prediction for kinesin light chain 2 (Q9H0B6) · a predicted model of the same protein · chain A against A, TM-score 0.79

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