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Solution NMR structure of the CBX3 in complex with H3K9ME3 peptide

Analyse Solution NMR structure of the CBX3 in complex with H3K9ME3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2L11
Type
protein
Length
69 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chromobox protein homolog 3; Histone H3
UniProt
Q13185, Q92133

Structure

solution nmr · 2 distinct chains · 16% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChromobox protein homolog 3protein5420% helix, 46% strandQ13185
BHistone H3protein150% helix, 27% strandQ92133

Interfaces

1 interface between chains.

  • A–B · 694 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 2L11 · Solution NMR structure of the Cbx3 in complex with H3K9me3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13185 · AlphaFold monomer V2.0 prediction for chromobox protein homolog 3 (Q13185) · a predicted model of the same protein · chain A against A, TM-score 0.90

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