Research workbench

BAZ2A bromodomain in complex with N-acetylpiperazine derivative fragment 18

Analyse BAZ2A bromodomain in complex with N-acetylpiperazine derivative fragment 18 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7R01
Type: protein
Length: 103 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.256
Source: Homo sapiens
Molecule: Bromodomain adjacent to zinc finger domain protein 2A
UniProt: Q9UIF9
Ligands: GI7, MG
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · resolution 2.256 · 1 distinct chain · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bromodomain adjacent to zinc finger domain protein 2A	protein	103	68% helix, 0% strand	Q9UIF9

Ligands and binding sites

GI7 · 1-[4-(4-ethanoylpiperazin-1-yl)phenyl]guanidine · ligand · chains A
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 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	79	0.42	0.79	19	GI7

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 0.98

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 Q9UIF9
Elsewhere: RCSB PDB 7R01 · PDBe 7R01 · UniProt Q9UIF9

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