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Complex structure of eed and trimethylated H3K9

Analyse Complex structure of eed and trimethylated H3K9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K27
Type: protein
Length: 367 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polycomb protein eed; Histone peptide
UniProt: O75530
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polycomb protein eed	protein	360	6% helix, 46% strand	O75530
B	Histone peptide	protein	7	0% helix, 0% strand	—

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	412	0.77	0.86	43	empty
2	97	0.38	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 427 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

3K27 · Complex structure of EED and trimethylated H3K9 · the same entry in another collection · chain A against A, TM-score 1.00
O75530 · AlphaFold monomer V2.0 prediction for polycomb protein eed (O75530) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O75530
Elsewhere: RCSB PDB 3K27 · PDBe 3K27 · UniProt O75530

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