Magnesium 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:

Chlorine	(Cl)	7 atoms
Fluorine	(F)	1 atom
Calcium	(Ca)	12 atoms

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

Magnesium binding site 1 out of 5 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg702 b:11.9 occ:0.64 O A:HOH1340 2.0 19.8 1.0 O A:HOH1516 2.1 22.0 1.0 O A:HOH926 2.1 19.9 1.0 O A:HOH845 2.1 18.0 1.0 O A:HOH1071 2.1 19.2 1.0 OD1 A:ASP562 2.2 11.9 1.0 CG A:ASP562 3.2 11.5 1.0 OD2 A:ASP562 3.5 12.6 1.0 O A:ILE563 3.8 13.8 1.0 O A:HOH1087 3.9 18.3 1.0 O A:HOH1570 4.2 31.0 1.0 O A:HOH1527 4.3 15.4 1.0 O A:HOH1161 4.3 13.9 1.0 OE1 A:GLU504 4.3 12.6 1.0 O A:HOH1400 4.3 40.0 1.0 N A:ILE563 4.4 10.1 1.0 O A:HOH1287 4.5 31.5 1.0 O A:HOH1131 4.6 41.0 1.0 CB A:ASP562 4.6 11.2 1.0 CD A:GLU504 4.7 11.1 1.0 C A:ILE563 4.8 11.8 1.0 O A:HOH810 4.8 45.2 1.0 O A:HOH1256 4.9 38.9 1.0 CG A:GLU504 4.9 10.8 1.0 CA A:ASP562 4.9 10.2 1.0

Magnesium binding site 2 out of 5 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg703 b:35.0 occ:1.00 O A:THR171 2.2 31.5 1.0 O A:TYR218 2.3 26.8 1.0 O A:HOH1007 2.4 29.1 1.0 O A:ASP169 2.5 35.7 1.0 O A:HOH1328 2.6 43.9 1.0 O A:HOH1438 2.7 49.8 1.0 C A:THR171 3.4 30.8 1.0 C A:TYR218 3.4 26.7 1.0 C A:ASP169 3.6 35.9 1.0 N A:THR171 3.9 34.4 1.0 N A:TYR218 3.9 30.5 1.0 OD1 A:ASP169 4.1 33.7 1.0 N A:ASP169 4.1 33.8 1.0 C A:GLU170 4.2 36.9 1.0 CA A:THR171 4.3 33.1 1.0 CA A:TYR218 4.3 28.4 1.0 N A:ASP219 4.3 24.3 1.0 N A:LEU172 4.4 28.1 1.0 CA A:LEU172 4.4 27.2 1.0 CB A:ASP219 4.5 22.7 1.0 N A:GLY173 4.5 24.3 1.0 CA A:ASP219 4.5 22.9 1.0 N A:GLU170 4.5 36.8 1.0 CA A:ASP169 4.5 34.8 1.0 C A:LEU172 4.5 25.8 1.0 CA A:GLU170 4.6 37.2 0.4 OD2 A:ASP219 4.6 22.3 1.0 CA A:GLU170 4.6 37.1 0.6 C A:GLY217 4.7 33.6 1.0 O A:GLU170 4.8 38.4 1.0 OG1 A:THR171 4.9 32.2 1.0 CG A:ASP219 5.0 21.4 1.0

Magnesium binding site 3 out of 5 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg704 b:22.7 occ:0.63 O A:HOH1075 1.9 30.4 1.0 O A:HOH1585 2.0 27.8 0.7 O A:HOH1589 2.0 32.7 1.0 O A:HOH1359 2.1 25.8 0.7 O A:HOH1521 2.2 35.1 1.0 O A:HOH1590 2.3 25.4 1.0 MG A:MG706 3.0 20.0 0.6 O A:HOH1112 4.0 33.5 1.0 O A:HOH889 4.0 27.1 1.0 O A:HOH1152 4.1 21.6 1.0 O A:HOH823 4.1 34.2 1.0 O A:HOH1482 4.1 41.5 1.0 O A:HOH1536 4.2 35.9 1.0 OE1 A:GLU253 4.4 17.2 1.0 O A:HOH1248 4.4 26.4 1.0 O A:HOH1375 4.7 29.4 1.0 O A:HOH1325 4.7 45.9 1.0 OD1 A:ASN661 4.9 25.9 0.3

Magnesium binding site 4 out of 5 in the Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg705 b:41.4 occ:1.00 O A:HOH1504 1.9 38.7 1.0 O A:HOH1399 2.0 38.6 1.0 O A:HOH902 2.2 38.6 1.0 O A:THR469 2.3 24.6 1.0 O A:HOH1443 2.4 48.6 1.0 C A:THR469 3.2 23.0 1.0 CA A:THR469 3.5 23.4 1.0 CB A:THR469 3.7 25.9 1.0 O A:PRO142 4.4 29.5 0.5 N A:ALA470 4.5 20.3 1.0 CG2 A:ILE141 4.6 29.1 0.5 OG1 A:THR469 4.7 27.4 1.0 O A:HOH886 4.7 42.7 1.0 CG2 A:THR469 4.8 27.3 1.0 N A:THR469 4.9 21.8 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Friedel-Crafts Alkylation Enzyme Cylk Mutant H391A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg706 b:20.0 occ:0.56 O A:HOH1075 1.8 30.4 1.0 O A:HOH1375 2.1 29.4 1.0 OE1 A:GLU253 2.1 17.2 1.0 O A:HOH889 2.3 27.1 1.0 O A:HOH1112 2.8 33.5 1.0 O A:HOH1359 2.8 25.8 0.7 MG A:MG704 3.0 22.7 0.6 CD A:GLU253 3.2 15.2 1.0 O A:HOH1589 3.6 32.7 1.0 OE2 A:GLU253 3.8 15.1 1.0 N A:HIS254 4.0 11.6 1.0 O A:HOH1285 4.0 27.0 1.0 O A:HOH1521 4.0 35.1 1.0 CA A:GLU253 4.0 11.4 1.0 O A:HOH823 4.1 34.2 1.0 CG A:GLU253 4.4 12.9 1.0 O A:HIS254 4.4 12.6 1.0 O A:HOH1152 4.5 21.6 1.0 CB A:GLU253 4.5 12.3 1.0 C A:GLU253 4.5 11.7 1.0 O A:HOH1590 4.6 25.4 1.0 O A:ALA252 4.6 15.0 1.0 OD1 A:ASN661 4.8 25.9 0.3 O A:HOH1585 4.9 27.8 0.7 O A:HOH1172 5.0 20.3 1.0 CA A:HIS254 5.0 11.6 1.0 O A:HOH1536 5.0 35.9 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