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Bromodomain of human TAF1 (2) with naphthyridinone compound

Analyse Bromodomain of human TAF1 (2) with naphthyridinone compound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P4S
Type: protein
Length: 134 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 2A of transcription initiation factor tfiid subunit 1
EC: 2.3.1.48, 2.7.11.1
UniProt: P21675
Ligands: 5LV
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isoform 2A of transcription initiation factor tfiid subunit 1 (EC 2.3.1.48, 2.7.11.1)	protein	134	72% helix, 0% strand	P21675

Ligands and binding sites

5LV · 8-[[1-(3-azanylpropyl)piperidin-4-yl]amino]-5-[5-(hydroxymethyl)pyridin-3-yl]-3-methyl-1~{H}-1,7-naphthyridin-2-one · 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	103	0.49	0.81	18	5LV

Compared structures

7P4S · BROMODOMAIN OF HUMAN TAF1 (2) WITH naphthyridi compound · 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 7P4S · PDBe 7P4S · UniProt P21675

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