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Crystal structure of the complex between human chromobox homolog 1 (CBX1) and H3K9ME3 peptide

Analyse Crystal structure of the complex between human chromobox homolog 1 (CBX1) and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6D07
Type
protein
Length
122 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chromobox protein homolog 1; Histone H3.1
UniProt
P83916, P68431
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 4 distinct chains · 25% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChromobox protein homolog 1protein5431% helix, 50% strandP83916
BChromobox protein homolog 1protein5227% helix, 52% strandP83916
CHistone H3.1protein90% helix, 33% strandP68431
DHistone H3.1protein70% helix, 43% strandP68431

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.360.7420empty

Interfaces

3 interfaces between chains.

  • A–C · 662 Ų buried · 20 hydrogen bonds · protein-protein
  • B–D · 625 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 321 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (methylation).

Compared structures

  • 6D07 · Crystal structure of the complex between human chromobox homolog 1 (CBX1) and H3K9me3… · the same entry in another collection · chain A against A, TM-score 1.00
  • P83916 · AlphaFold monomer V2.0 prediction for chromobox protein homolog 1 (P83916) · a predicted model of the same protein · chain B against A, TM-score 0.96

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