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Crystal structure of the bromodomain (bd) of human bromodomain and phd finger-containing transcription factor (bptf) bound to compound 4 (SKT1174)

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

PDB: 7K6S
Type: protein
Length: 117 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleosome-remodeling factor subunit bptf
UniProt: Q12830
Ligands: VYM, CL
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleosome-remodeling factor subunit bptf	protein	117	67% helix, 2% strand	Q12830

Ligands and binding sites

VYM · (7-amino-3,4-dihydroquinolin-1(2H)-yl)(cyclopropyl) methanone · ligand · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · chains A
GOL · Glycerol · 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	86	0.52	0.83	17	VYM

Compared structures

7K6S · Crystal structure of the bromodomain (BD) of human Bromodomain and PHD finger-containing… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q12830
Elsewhere: RCSB PDB 7K6S · PDBe 7K6S · UniProt Q12830

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