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Development of synthetically accessible non-secosteroidal hybrid molecules combining vitamin D receptor agonism and histone deacetylase inhibition

Analyse Development of synthetically accessible non-secosteroidal hybrid molecules… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FHI
Type: protein
Length: 248 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vitamin nuclear receptor; Src-1
Ligands: 0S4
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vitamin nuclear receptor	protein	238	64% helix, 3% strand	—
B	Src-1	protein	10	70% helix, 0% strand	—

Ligands and binding sites

0S4 · N-hydroxy-2-{4-[3-(4-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}-3-methylphenyl)pentan-3-yl]-2-methylphenoxy}acetamide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	332	0.86	0.95	38	0S4
2	152	0.43	0.75	29	empty

Interfaces

1 interface between chains.

A–B · 557 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4FHI · Development of synthetically accessible non-secosteroidal hybrid molecules combining… · 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
Elsewhere: RCSB PDB 4FHI · PDBe 4FHI

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