Fluorine in PDB 7fh7: Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F

The structure of Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F, PDB code: 7fh7 was solved by H.Q.Wang, Z.Wei, Z.Xiang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.30 / 1.42
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.61, 78.37, 127, 90, 90, 90
R / Rfree (%)	13.5 / 17.9

The structure of Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F also contains other interesting chemical elements:

Chlorine	(Cl)	7 atoms
Magnesium	(Mg)	4 atoms
Calcium	(Ca)	12 atoms

The binding sites of Fluorine atom in the Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F (pdb code 7fh7). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F, PDB code: 7fh7:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F within 5.0Å range: probe atom residue distance (Å) B Occ A:F1001 b:50.8 occ:0.95 F06 A:4ON1001 0.0 50.8 0.9 C05 A:4ON1001 1.4 50.5 0.9 C04 A:4ON1001 2.4 50.6 0.9 C07 A:4ON1001 2.4 49.0 0.9 OD2 A:ASP440 2.9 18.4 1.0 C08 A:4ON1001 2.9 46.7 0.9 C19 A:4ON1002 3.0 15.6 0.5 O20 A:4ON1002 3.1 9.6 0.5 C18 A:4ON1002 3.1 18.7 0.5 CL A:CL1019 3.4 17.1 1.0 C03 A:4ON1001 3.4 50.9 0.9 CD1 A:LEU438 3.6 15.8 1.0 C21 A:4ON1002 3.8 18.6 0.5 C16 A:4ON1002 3.9 21.6 0.5 OH A:TYR473 3.9 16.0 1.0 CG A:ASP440 3.9 14.6 1.0 O A:HOH1364 4.2 15.2 1.0 OD1 A:ASP440 4.3 14.6 1.0 C09 A:4ON1001 4.4 43.5 0.9 NH1 A:ARG105 4.4 15.9 1.0 C14 A:4ON1002 4.5 20.3 0.5 C15 A:4ON1002 4.6 21.8 0.5 CG A:LEU438 4.6 14.8 1.0 C02 A:4ON1001 4.6 50.8 0.9 O17 A:4ON1002 4.7 21.8 0.5 CD2 A:LEU438 4.9 16.5 1.0

Fluorine binding site 2 out of 3 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F within 5.0Å range: probe atom residue distance (Å) B Occ A:F1002 b:25.5 occ:0.50 F06 A:4ON1002 0.0 25.5 0.5 C05 A:4ON1002 1.4 26.0 0.5 C07 A:4ON1002 2.3 26.4 0.5 C04 A:4ON1002 2.4 25.0 0.5 CG A:PRO412 3.5 22.3 1.0 CD A:PRO412 3.6 22.3 1.0 CB A:PRO412 3.7 19.6 1.0 C08 A:4ON1002 3.7 26.8 0.5 CD1 A:LEU411 3.8 33.2 1.0 CD1 A:PHE63 3.9 21.9 1.0 CG A:LEU411 4.1 32.5 1.0 CE1 A:PHE63 4.1 21.1 1.0 CG A:PRO73 4.1 15.5 1.0 CD2 A:PHE72 4.3 22.2 1.0 O A:PRO412 4.3 18.4 1.0 N A:PRO412 4.3 18.8 1.0 CD A:PRO73 4.5 18.3 1.0 CA A:PRO412 4.6 18.4 1.0 CD2 A:LEU411 4.8 33.9 1.0 CE2 A:PHE72 4.8 21.6 1.0 N A:PRO73 4.8 17.0 1.0 CA A:PRO73 4.8 16.6 1.0 C A:PRO412 4.8 17.2 1.0 C09 A:4ON1002 4.9 26.2 0.5 CB A:PRO73 4.9 15.1 1.0

Fluorine binding site 3 out of 3 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Friedel-Crafts Alkylation Enzyme Cylk Mutant Y37F within 5.0Å range: probe atom residue distance (Å) B Occ A:F1002 b:31.9 occ:0.50 F06 A:4ON1002 0.0 31.9 0.5 C05 A:4ON1002 1.4 30.7 0.5 C04 A:4ON1002 2.3 29.7 0.5 C07 A:4ON1002 2.3 29.7 0.5 C03 A:4ON1002 2.6 27.5 0.5 CG2 A:ILE101 3.5 21.9 1.0 C08 A:4ON1002 3.7 28.8 0.5 CD1 A:LEU130 3.8 22.3 1.0 C02 A:4ON1002 3.8 25.9 0.5 CZ A:PHE76 4.0 27.3 1.0 CE3 A:TRP103 4.1 16.1 1.0 CE1 A:PHE76 4.2 27.3 1.0 CD2 A:TRP103 4.2 15.7 1.0 C01 A:4ON1002 4.3 25.3 0.5 CG A:TRP103 4.4 15.6 1.0 CB A:TRP103 4.5 15.0 1.0 CZ3 A:TRP103 4.7 18.1 1.0 CB A:ILE101 4.7 20.1 1.0 C09 A:4ON1002 4.8 28.7 0.5 CD1 A:ILE101 4.9 22.4 1.0 CE2 A:TRP103 4.9 15.0 1.0

H.Q.Wang, S.B.Mou, W.Xiao, H.Zhou, X.D.Hou, S.J.Wang, Q.Wang, J.Gao, Z.Wei, L.Liu, Z.Xiang. Structural Basis For the Friedel-Crafts Alkylation in Cylindrocyclophane Biosynthesis Acs Catal. V. 12 2108 2022.
DOI: 10.1021/ACSCATAL.1C04816