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Crystal structure of human bromodomain containing protein 3 (BRD3)

Analyse Crystal structure of human bromodomain containing protein 3 (BRD3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NXB
Type
protein
Length
232 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bromodomain-containing protein 3
UniProt
Q15059
Ligands
NA
Pockets
4 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABromodomain-containing protein 3protein11160% helix, 0% strandQ15059
BBromodomain-containing protein 3protein12155% helix, 0% strandQ15059

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · 7 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12810.590.7829empty
21090.520.8220EDO
31070.450.7819empty
4610.340.7716empty

Interfaces

1 interface between chains.

  • A–B · 856 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 2NXB · Crystal structure of human Bromodomain containing protein 3 (BRD3) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q15059 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 3 (Q15059) · a predicted model of the same protein · chain B against A, TM-score 0.97

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