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Crystal structure of the essential inner kinetochore protein CEP3P

Analyse Crystal structure of the essential inner kinetochore protein CEP3P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QUQ
Type
protein
Length
517 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Centromere DNA-binding protein complex CBF3 subunit B
UniProt
P40969
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACentromere DNA-binding protein complex CBF3 subunit Bprotein51769% helix, 1% strandP40969

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13770.780.8850empty
21340.610.8523empty
31190.450.7724empty
41220.400.7531empty
5980.370.7420empty

Compared structures

  • 2QUQ · Crystal Structure of the Essential Inner Kinetochore Protein Cep3p · the same entry in another collection · chain A against A, TM-score 1.00
  • P40969 · AlphaFold monomer V2.0 prediction for centromere DNA-binding protein complex CBF3 subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99

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