GL1X · GenesisL1 explorer

Research workbench

Structure of the chromodomain from mouse HP1BETA in complex with the lysine 9-methyl histone H3 N-terminal peptide, NMR, 25 structures

Analyse Structure of the chromodomain from mouse HP1BETA in complex with the lysine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GUW
Type
protein
Length
91 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chromobox protein homolog 1; Histone H3.1
UniProt
P23197, P16106

Structure

solution nmr · 2 distinct chains · 12% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChromobox protein homolog 1protein7315% helix, 21% strandP23197
BHistone H3.1protein180% helix, 11% strandP16106

Interfaces

1 interface between chains.

  • A–B · 763 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (methylation).

Compared structures

  • 1GUW · STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1beta IN COMPLEX WITH THE LYSINE 9-METHYL… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.