Human sterol 14A-demethylase (CYP51) in complex with the functionally irreversible inhibitor (R)-N-(1-(3-chloro-4'-fluoro-[1,1'-biphenyl]- 4-yl)-2-(1H-imidazol-1-YL)ETHYL)-4-(5-(3-fluoro-5-(5-fluoropyrimidin- 4-YL)PHENYL)-1,3,4-oxadiazol-2-YL)BENZAMIDE

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).

Ligands and binding sites

• DXC · (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid · ligand · 8 copies · chains A
• PJM · N-[(1R)-1-(3-chloro-4'-fluoro[1,1'-biphenyl]-4-yl)-2-(1H-imidazol-1-yl)ethyl]-4-{5-[3-fluoro-5-(5-fluoropyrimidin-4-yl)phenyl]-1,3,4-oxadiazol-2-yl}benzamide · ligand · 3 copies · chains A, B
• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 356 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

• 6Q2T · Human sterol 14a-demethylase (CYP51) in complex with the functionally irreversible… · the same entry in another collection · chain A against A, TM-score 1.00
• Q16850 · AlphaFold monomer V2.0 prediction for lanosterol 14-alpha demethylase (Q16850) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q16850
• Elsewhere: RCSB PDB 6Q2T · PDBe 6Q2T · UniProt Q16850