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Solution structure of CHD4-PHD2 in complex with H3K9ME3

Analyse Solution structure of CHD4-PHD2 in complex with H3K9ME3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L75
Type: protein
Length: 67 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chromodomain-helicase-DNA-binding protein 4; 14-meric peptide from 1HISTONE H3.1
UniProt: Q14839, P68431
Ligands: ZN

Structure

solution nmr · 2 distinct chains · 0% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chromodomain-helicase-DNA-binding protein 4	protein	56	0% helix, 11% strand	Q14839
B	14-meric peptide from 1HISTONE H3.1	protein	11	0% helix, 36% strand	P68431

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 607 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

2L75 · Solution structure of CHD4-PHD2 in complex with H3K9me3 · the same entry in another collection · chain A against A, TM-score 1.00
Q14839 · AlphaFold monomer V2.0 prediction for chromodomain-helicase-DNA- binding protein 4… · a predicted model of the same protein · chain A against A, TM-score 0.85

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 Q14839
Every structure of UniProt P68431
Elsewhere: RCSB PDB 2L75 · PDBe 2L75 · UniProt Q14839 · UniProt P68431

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