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Structure of the chromodomain of MRG2 in complex with H3K4ME3

Analyse Structure of the chromodomain of MRG2 in complex with H3K4ME3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PL6
Type: protein
Length: 114 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AT1G02740
UniProt: Q4V3E2
Ligands: M3L

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	AT1G02740	protein	57	11% helix, 58% strand	Q4V3E2

Ligands and binding sites

M3L · N-trimethyllysine · ligand · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 471 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4PL6 · Structure of the chromodomain of MRG2 in complex with H3K4me3 · the same entry in another collection · chain A against A, TM-score 1.00
Q4V3E2 · AlphaFold monomer V2.0 prediction for protein MRG2 (Q4V3E2) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q4V3E2
Elsewhere: RCSB PDB 4PL6 · PDBe 4PL6 · UniProt Q4V3E2

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