Fluorine in PDB 4ze0: Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole, PDB code: 4ze0 was solved by A.Sagatova, M.V.Keniya, R.Wilson, J.D.A.Tyndall, B.C.Monk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.16 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.220, 66.550, 80.900, 90.00, 98.67, 90.00
R / Rfree (%)	19.2 / 23.9

The structure of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Fluorine atom in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole (pdb code 4ze0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole, PDB code: 4ze0:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:28.0 occ:1.00 F1 A:VOR602 0.0 28.0 1.0 C16 A:VOR602 1.3 28.7 1.0 C19 A:VOR602 2.3 29.3 1.0 C13 A:VOR602 2.4 28.9 1.0 C10 A:VOR602 2.9 31.6 1.0 C11 A:VOR602 3.0 31.2 1.0 C12 A:VOR602 3.0 28.0 1.0 C22 A:VOR602 3.6 30.3 1.0 N7 A:VOR602 3.6 26.7 1.0 C17 A:VOR602 3.6 28.5 1.0 CZ A:PHE236 3.6 49.3 1.0 N5 A:VOR602 3.6 28.7 1.0 CA A:GLY314 3.6 29.3 1.0 C14 A:VOR602 3.8 36.8 1.0 CZ A:PHE134 3.8 35.8 1.0 CE1 A:PHE236 4.1 47.2 1.0 C20 A:VOR602 4.1 26.9 1.0 C15 A:VOR602 4.2 32.6 1.0 N A:GLY314 4.2 26.3 1.0 O4 A:VOR602 4.3 29.7 1.0 N6 A:VOR602 4.3 33.4 1.0 CE2 A:PHE134 4.4 34.8 1.0 CE2 A:PHE236 4.6 45.7 1.0 F3 A:VOR602 4.7 28.9 1.0 O A:GLY310 4.7 29.0 1.0 C25 A:VOR602 4.7 24.1 1.0 C21 A:VOR602 4.8 24.0 1.0 CE1 A:PHE134 4.9 35.6 1.0 C A:GLY314 5.0 26.1 1.0

Fluorine binding site 2 out of 3 in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:43.1 occ:1.00 F2 A:VOR602 0.0 43.1 1.0 C18 A:VOR602 1.4 37.3 1.0 C23 A:VOR602 2.4 34.1 1.0 C15 A:VOR602 2.4 32.6 1.0 O4 A:VOR602 2.7 29.7 1.0 C11 A:VOR602 2.9 31.2 1.0 C14 A:VOR602 3.0 36.8 1.0 O A:HOH886 3.1 31.5 1.0 C10 A:VOR602 3.3 31.6 1.0 CZ A:TYR126 3.6 43.3 1.0 CE2 A:TYR126 3.6 43.5 1.0 N9 A:VOR602 3.6 36.5 1.0 N6 A:VOR602 3.6 33.4 1.0 OH A:TYR126 3.7 51.7 1.0 O1A A:HEM601 3.7 28.2 1.0 C24 A:VOR602 4.0 37.8 1.0 CD2 A:LEU383 4.0 32.2 1.0 CE1 A:TYR126 4.1 43.5 1.0 C12 A:VOR602 4.1 28.0 1.0 CD2 A:TYR126 4.2 42.1 1.0 CBA A:HEM601 4.2 25.8 1.0 CGA A:HEM601 4.5 28.4 1.0 C13 A:VOR602 4.6 28.9 1.0 CD1 A:TYR126 4.6 45.7 1.0 CG A:TYR126 4.6 38.9 1.0 CD1 A:LEU380 4.7 33.1 1.0 C17 A:VOR602 5.0 28.5 1.0

Fluorine binding site 3 out of 3 in the Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Saccharomyces Cerevisiae CYP51 (Lanosterol 14-Alpha Demethylase) Y140F Mutant Complexed with Voriconazole within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:28.9 occ:1.00 F3 A:VOR602 0.0 28.9 1.0 C22 A:VOR602 1.4 30.3 1.0 C19 A:VOR602 2.3 29.3 1.0 C20 A:VOR602 2.3 26.9 1.0 O A:GLY310 3.4 29.0 1.0 C A:GLY310 3.5 31.6 1.0 C16 A:VOR602 3.6 28.7 1.0 CD1 A:ILE139 3.6 41.2 1.0 C17 A:VOR602 3.6 28.5 1.0 N A:VAL311 3.8 30.1 1.0 CA A:VAL311 3.9 31.9 1.0 CMD A:HEM601 4.1 21.6 1.0 C13 A:VOR602 4.1 28.9 1.0 CA A:GLY310 4.2 28.9 1.0 CG2 A:VAL311 4.3 22.3 1.0 CG2 A:ILE139 4.3 26.6 1.0 CG1 A:ILE139 4.5 33.8 1.0 C2D A:HEM601 4.5 28.0 1.0 CE2 A:PHE134 4.6 34.8 1.0 F1 A:VOR602 4.7 28.0 1.0 CB A:VAL311 4.8 30.7 1.0 C1D A:HEM601 4.9 23.5 1.0 C A:VAL311 5.0 31.1 1.0

A.A.Sagatova, M.V.Keniya, R.K.Wilson, M.Sabherwal, J.D.Tyndall, B.C.Monk. Triazole Resistance Mediated By Mutations of A Conserved Active Site Tyrosine in Fungal Lanosterol 14 Alpha-Demethylase. Sci Rep V. 6 26213 2016.
ISSN: ESSN 2045-2322
PubMed: 27188873
DOI: 10.1038/SREP26213