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The crystal structure of the minimal functional domain of the microtubule destabilizer KIF2C complexed with mg-ADP

Analyse The crystal structure of the minimal functional domain of the microtubule… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1V8J
Type
protein
Length
337 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin-like protein KIF2C
UniProt
Q922S8
Ligands
ADP, MG
Pockets
4 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin-like protein KIF2Cprotein33736% helix, 27% strandQ922S8

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11790.540.7930empty
21800.520.7824empty
31550.490.7721empty
41440.460.7738MG, ADP

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1V8J · The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q922S8 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF2C (Q922S8) · a predicted model of the same protein · chain A against A, TM-score 0.92

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