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Symmetric dimethylation of H3 arginine 2 is a novel histone mark that supports euchromatin maintenance

Analyse Symmetric dimethylation of H3 arginine 2 is a novel histone mark that supports… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4A7J
Type
protein
Length
309 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Wd repeat-containing protein 5; Histone H3.1T
UniProt
P61964, Q16695
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AWd repeat-containing protein 5protein3030% helix, 52% strandP61964
BHistone H3.1Tprotein60% helix, 0% strandQ16695

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15130.730.8144empty

Interfaces

1 interface between chains.

  • A–B · 575 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 4A7J · Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q16695 · AlphaFold monomer V2.0 prediction for histone H3.1T (Q16695) · a predicted model of the same protein · chain B against A, TM-score 0.43

Analyse

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