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Crystal structure of the second bromodomain (BD2) of human TAF1 bound to ZS1-580

Analyse Crystal structure of the second bromodomain (BD2) of human TAF1 bound to ZS1-580 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LB3
Type: protein
Length: 137 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription initiation factor tfiid subunit 1
UniProt: P21675
Ligands: XXS
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription initiation factor tfiid subunit 1	protein	137	73% helix, 0% strand	P21675

Ligands and binding sites

XXS · 4-{4-[(3R)-3-methylmorpholin-4-yl]-6-[1-(S-methylsulfonimidoyl)cyclopropyl]pyrimidin-2-yl}-1H-indazole · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.51	0.81	21	XXS

Compared structures

7LB3 · Crystal structure of the second bromodomain (BD2) of human TAF1 bound to ZS1-580 · the same entry in another collection · chain A against A, TM-score 1.00

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 P21675
Elsewhere: RCSB PDB 7LB3 · PDBe 7LB3 · UniProt P21675

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