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

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
1V8K
Type
protein
Length
332 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin-like protein KIF2C
UniProt
Q922S8
Ligands
ANP, MG
Pockets
4 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin-like protein KIF2Cprotein33236% helix, 29% strandQ922S8

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.500.7629empty
21380.440.7625empty
31390.430.7628MG, ANP
4890.400.7715empty

Compared structures

  • 1V8K · 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 0.91

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