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BAZ2A bromodomain in complex with acetylpyrrole derivative compound 78

Analyse BAZ2A bromodomain in complex with acetylpyrrole derivative compound 78 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QYE
Type: protein
Length: 105 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.65
Source: Homo sapiens
Molecule: Bromodomain adjacent to zinc finger domain protein 2A
UniProt: Q9UIF9
Ligands: GQF
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · resolution 1.65 · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain adjacent to zinc finger domain protein 2A	protein	105	65% helix, 0% strand	Q9UIF9

Ligands and binding sites

GQF · 1-[4-cyclopentyl-2-methyl-5-(2-piperazin-1-yl-1,3-thiazol-4-yl)-1~{H}-pyrrol-3-yl]ethanone · ligand · 2 copies · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.47	0.80	17	GQF

Compared structures

Q9UIF9 · AlphaFold monomer V2.0 prediction for bromodomain adjacent to zinc finger domain protein… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9UIF9
Elsewhere: RCSB PDB 7QYE · PDBe 7QYE · UniProt Q9UIF9

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