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Crystal structure of the motor domain of human kinesin family member 22

Analyse Crystal structure of the motor domain of human kinesin family member 22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6NJE
Type
protein
Length
297 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin-like protein KIF22
UniProt
Q14807
Ligands
ADP, MG, NA, CL
Pockets
4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin-like protein KIF22protein29730% helix, 29% strandQ14807

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • NA · Sodium ion · metal · chains A
  • CL · Chloride ion · ion · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11410.510.8032MG
2740.420.8017empty
31230.360.7328CL
4770.350.7614empty

Compared structures

  • 6NJE · Crystal structure of the motor domain of human kinesin family member 22 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q14807 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF22 (Q14807) · a predicted model of the same protein · chain A against A, TM-score 0.91

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