Chlorine in PDB 7fh8: Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A

The structure of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A, PDB code: 7fh8 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)	23.90 / 1.32
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.28, 78.46, 126.29, 90, 90, 90
R / Rfree (%)	12.1 / 15.4

The structure of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Magnesium	(Mg)	5 atoms
Calcium	(Ca)	12 atoms

The binding sites of Chlorine atom in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A (pdb code 7fh8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 7 binding sites of Chlorine where determined in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A, PDB code: 7fh8:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


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Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl719 b:15.7 occ:1.00 O A:HOH1028 2.6 24.5 0.3 OH A:TYR473 3.0 13.8 1.0 NH1 A:ARG105 3.3 13.7 1.0 O A:HOH1028 3.3 13.6 0.7 CA A:THR84 3.5 11.3 1.0 CB A:THR84 3.5 11.5 1.0 CE2 A:TYR473 3.6 12.3 1.0 CE2 A:PHE499 3.7 12.8 1.0 CZ A:TYR473 3.8 12.9 1.0 N A:VAL85 3.9 11.3 1.0 CG2 A:THR84 3.9 12.8 1.0 C A:THR84 4.2 11.3 1.0 CZ A:ARG105 4.3 13.2 1.0 O A:LEU83 4.3 13.4 1.0 CZ A:PHE499 4.4 13.1 1.0 OD2 A:ASP440 4.4 13.4 0.5 CG2 A:VAL85 4.4 14.1 1.0 NH2 A:ARG105 4.4 14.5 1.0 OD2 A:ASP440 4.4 19.2 0.5 N A:THR84 4.6 12.0 1.0 CD2 A:PHE499 4.7 11.8 1.0 OG1 A:THR84 4.8 11.6 1.0 C A:LEU83 4.8 12.2 1.0 O A:HOH874 4.9 46.8 1.0 C24 A:4PJ701 4.9 26.7 0.8 CD2 A:TYR473 4.9 12.1 1.0

Chlorine binding site 2 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl720 b:24.4 occ:1.00 O A:HOH1432 2.9 33.2 1.0 N A:THR247 3.2 13.4 1.0 O A:HOH891 3.2 31.7 1.0 O A:HOH1114 3.4 15.9 1.0 CG A:LYS246 3.7 20.1 0.5 CA A:LYS246 3.8 14.4 0.5 CA A:LYS246 3.8 14.8 0.5 OG1 A:THR247 3.8 12.9 1.0 CB A:THR247 3.9 13.2 1.0 C A:LYS246 4.0 13.6 1.0 CB A:LYS246 4.0 16.3 0.5 CA A:THR247 4.1 12.2 1.0 CB A:LYS246 4.2 17.3 0.5 NZ A:LYS246 4.4 25.8 0.5 CG A:LYS246 4.5 18.5 0.5 O A:HOH965 4.6 15.1 1.0 O A:THR247 4.7 14.0 1.0 CD A:LYS246 4.9 22.9 0.5 C A:THR247 5.0 11.9 1.0

Chlorine binding site 3 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl721 b:28.0 occ:1.00 O A:HOH1582 2.9 46.8 1.0 N A:SER461 3.1 14.1 1.0 O A:HOH1276 3.4 25.3 1.0 CA A:GLY460 3.5 13.2 1.0 CB A:THR435 3.8 14.7 1.0 C A:GLY460 3.8 13.0 1.0 O A:HOH1041 4.0 35.1 1.0 CG2 A:THR435 4.0 15.6 1.0 CA A:SER461 4.1 14.2 1.0 CB A:SER461 4.2 16.0 1.0 O A:SER461 4.2 16.8 1.0 OG1 A:THR435 4.3 14.5 1.0 C A:SER461 4.4 14.4 1.0 CG2 A:THR437 4.5 14.3 1.0 OG A:SER461 4.7 17.4 1.0 CG2 A:ILE436 4.9 18.3 1.0 N A:GLY460 4.9 13.2 1.0 N A:ILE436 4.9 14.4 1.0 CA A:THR435 5.0 13.6 1.0

Chlorine binding site 4 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl722 b:29.3 occ:1.00 O A:HOH967 3.0 24.8 1.0 N A:GLY148 3.1 20.3 1.0 N A:GLN137 3.3 26.2 0.5 CB A:GLN137 3.4 30.8 0.5 CA A:GLN137 3.5 28.9 0.5 C A:GLU136 3.8 23.7 0.5 CG A:GLN137 3.8 31.3 0.5 N A:GLN137 3.8 23.7 0.5 CA A:ALA147 3.9 19.0 1.0 CA A:GLY148 4.0 20.7 1.0 CB A:GLU136 4.0 17.8 0.5 CB A:GLU136 4.0 17.3 0.5 C A:GLU136 4.0 21.3 0.5 CA A:GLN137 4.0 27.9 0.5 C A:ALA147 4.0 19.3 1.0 CG1 A:ILE134 4.0 16.3 1.0 CD1 A:ILE134 4.1 16.9 1.0 O A:GLU136 4.1 25.2 0.5 O A:GLU136 4.3 21.5 0.5 O A:ASN146 4.4 18.8 1.0 CG A:GLN137 4.4 32.8 0.5 CB A:GLN137 4.5 29.6 0.5 CA A:GLU136 4.5 19.3 0.5 CA A:GLU136 4.6 17.9 0.5 O A:HOH850 4.7 22.9 1.0 CB A:ALA147 4.7 21.5 1.0 OE1 A:GLN137 4.7 35.6 0.5 C A:GLY148 4.8 22.2 1.0 N A:LYS149 4.8 20.8 1.0 CD A:GLN137 4.9 33.5 0.5 CD A:GLN137 4.9 34.8 0.5 N A:ALA147 5.0 18.9 1.0

Chlorine binding site 5 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl723 b:31.4 occ:1.00 O A:HOH819 3.0 44.2 1.0 NH2 A:ARG306 3.1 28.6 0.4 NH1 A:ARG306 3.2 29.5 0.4 CZ A:ARG306 3.2 28.8 0.4 NZ A:LYS298 3.2 15.9 1.0 NE A:ARG306 3.6 24.8 0.6 CD1 A:TRP307 3.6 13.2 1.0 NE1 A:TRP307 3.7 13.2 1.0 CB A:ARG306 3.8 17.7 0.4 CB A:ARG306 3.8 15.3 0.6 O A:SER357 3.8 13.6 1.0 CD A:LYS298 3.9 13.3 1.0 CE A:LYS298 3.9 14.2 1.0 NE A:ARG306 3.9 27.0 0.4 NH2 A:ARG306 3.9 29.8 0.6 O A:HOH890 3.9 31.8 1.0 OD1 A:ASP358 4.2 25.8 1.0 CZ A:ARG306 4.2 28.4 0.6 CG A:ARG306 4.2 20.5 0.4 CG A:ARG306 4.3 17.3 0.6 O A:HOH995 4.5 39.1 1.0 CD A:ARG306 4.5 21.0 0.6 CA A:ASP358 4.6 14.4 1.0 CD A:ARG306 4.7 23.9 0.4 O A:HOH871 4.7 24.8 1.0 O A:HOH1183 4.8 26.0 1.0 C A:SER357 4.8 13.6 1.0 O A:HOH1182 4.9 36.5 1.0 CG A:TRP307 4.9 12.9 1.0 CE2 A:TRP307 5.0 12.7 1.0 CA A:ARG306 5.0 15.9 0.4

Chlorine binding site 6 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl724 b:37.2 occ:1.00 O A:HOH1341 2.9 49.8 1.0 O A:HOH1329 3.0 28.8 1.0 N A:LEU232 3.1 23.8 1.0 O A:HOH1496 3.2 46.7 1.0 CG A:LEU232 3.7 23.1 1.0 CA A:SER231 3.7 24.4 1.0 CB A:LEU232 3.8 23.4 1.0 C A:SER231 3.9 23.5 1.0 CD1 A:LEU232 3.9 23.8 1.0 CD1 A:LEU201 4.0 24.4 1.0 CA A:LEU232 4.0 24.2 1.0 O A:HOH836 4.2 44.5 1.0 O A:LEU230 4.3 24.3 1.0 OG A:SER231 4.4 28.3 1.0 CG A:LEU201 4.4 23.2 1.0 CB A:SER231 4.5 25.8 1.0 O A:HOH1349 4.6 35.6 1.0 CB A:LEU201 4.7 23.5 1.0 N A:SER231 4.8 24.0 1.0 O A:HOH808 4.9 42.2 1.0 C A:LEU230 4.9 24.2 1.0

Chlorine binding site 7 out of 7 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl725 b:105.2 occ:1.00 O A:HOH1278 3.4 34.2 1.0 N A:LEU172 3.5 28.1 1.0 CB A:LEU172 3.7 28.3 1.0 CD1 A:LEU174 3.7 24.6 1.0 CB A:THR171 3.9 33.2 1.0 CG A:LEU174 3.9 23.6 1.0 CA A:LEU172 4.1 27.2 1.0 CG A:LEU172 4.2 30.1 1.0 CA A:THR171 4.4 33.1 1.0 C A:THR171 4.4 30.8 1.0 OG1 A:THR171 4.5 32.2 1.0 CD1 A:LEU172 4.6 31.6 1.0 CD A:LYS17 4.8 37.6 1.0 CB A:LEU174 4.8 22.4 1.0 C A:LEU172 4.8 25.8 1.0 CG2 A:THR171 4.9 34.2 1.0 N A:GLY173 4.9 24.3 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