Research workbench

Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9

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

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

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heterochromatin protein 1	protein	52	25% helix, 50% strand	P05205
P	Trimethylated histone H3	protein	6	0% helix, 33% strand	P02299

Interfaces

1 interface between chains.

A–P · 549 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

1KNE · Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 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 0.96
P02299 · AlphaFold monomer V2.0 prediction for histone H3 (P02299) · a predicted model of the same protein · chain P against A, TM-score 0.65

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 1KNE · PDBe 1KNE · UniProt P05205 · UniProt P02299

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