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Cystal structure of the DPY30 for MLL/SET1 compass H3K4 trimethylation

Analyse Cystal structure of the DPY30 for MLL/SET1 compass H3K4 trimethylation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RTA
Type
protein
Length
129 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein dpy-30 homolog
UniProt
Q9C005
Pockets
1 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein dpy-30 homologprotein5866% helix, 0% strandQ9C005
BProtein dpy-30 homologprotein7163% helix, 0% strandQ9C005

Ligands and binding sites

  • FMT · Formic acid · additive · 3 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1700.300.7314empty

Interfaces

1 interface between chains.

  • A–B · 1255 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 4RTA · Cystal structure of the Dpy30 for MLL/SET1 COMPASS H3K4 trimethylation · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9C005 · AlphaFold monomer V2.0 prediction for protein dpy-30 homolog (Q9C005) · a predicted model of the same protein · chain A against A, TM-score 0.88

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