Research workbench

Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.

Analyse Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KNA
Type: protein
Length: 58 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heterochromatin protein 1; Methylated histone H3
UniProt: P05205, P02299

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heterochromatin protein 1	protein	52	31% helix, 50% strand	P05205
P	Methylated histone H3	protein	6	0% helix, 33% strand	P02299

Interfaces

1 interface between chains.

A–P · 547 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

1KNA · Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9. · the same entry in another collection · chain A against A, TM-score 1.00
P05205 · AlphaFold monomer V2.0 prediction for heterochromatin protein 1 (P05205) · a predicted model of the same protein · chain A against A, TM-score 0.97
P02299 · AlphaFold monomer V2.0 prediction for histone H3 (P02299) · a predicted model of the same protein · chain P against A, TM-score 0.55

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P05205
Every structure of UniProt P02299
Elsewhere: RCSB PDB 1KNA · PDBe 1KNA · UniProt P05205 · UniProt P02299

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