Bromine in PDB 7roo: Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide

The structure of Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide, PDB code: 7roo was solved by T.B.Ruskoski, A.K.Boal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.78 / 1.52
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	93.47, 138.656, 99.511, 90, 90, 90
R / Rfree (%)	16.9 / 19.8

The structure of Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Sodium	(Na)	1 atom
Calcium	(Ca)	10 atoms

The binding sites of Bromine atom in the Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide (pdb code 7roo). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide, PDB code: 7roo:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br708 b:11.2 occ:0.84 OH A:TYR473 3.2 12.3 1.0 NH1 A:ARG105 3.3 10.4 1.0 O A:HOH875 3.4 12.2 1.0 CA A:THR84 3.6 8.8 1.0 CB A:THR84 3.6 8.7 1.0 O A:HOH1074 3.6 27.4 1.0 CE2 A:PHE499 3.8 9.7 1.0 CE2 A:TYR473 3.8 11.7 1.0 CZ A:TYR473 4.0 10.5 1.0 CG2 A:THR84 4.0 9.4 1.0 N A:VAL85 4.0 8.7 1.0 OD2 A:ASP440 4.2 18.7 1.0 CZ A:PHE499 4.3 9.4 1.0 C A:THR84 4.4 8.4 1.0 CZ A:ARG105 4.4 9.6 1.0 O A:LEU83 4.4 9.9 1.0 NH2 A:ARG105 4.5 10.3 1.0 CG2 A:VAL85 4.5 9.2 1.0 N A:THR84 4.8 8.3 1.0 CD2 A:PHE499 4.8 9.2 1.0 OG1 A:THR84 4.9 8.8 1.0 C A:LEU83 5.0 10.3 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br709 b:12.5 occ:0.70 O A:HOH1158 3.4 10.4 0.4 N A:GLY148 3.4 14.6 1.0 O A:HOH1156 3.4 30.4 1.0 O A:HOH937 3.6 27.0 1.0 O A:GLU136 3.7 12.3 1.0 C A:GLU136 3.7 11.1 1.0 N A:GLN137 3.8 10.8 1.0 CA A:GLN137 3.8 11.2 1.0 CG A:GLN137 3.9 12.0 1.0 CA A:ALA147 4.0 15.2 1.0 CB A:GLU136 4.0 12.6 1.0 C A:ALA147 4.2 14.5 1.0 CA A:GLY148 4.2 15.3 1.0 CB A:GLN137 4.4 11.4 1.0 CA A:GLU136 4.5 11.4 1.0 CB A:ALA147 4.6 15.4 1.0 O A:HOH807 4.7 5.2 1.0 O A:ASN146 5.0 15.1 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br710 b:14.6 occ:0.72 O A:HOH819 3.4 22.0 1.0 CG A:PRO48 3.8 25.7 1.0 CD A:PRO48 4.1 25.2 1.0 CB A:PRO48 4.2 25.4 1.0 CA A:GLY46 4.6 29.7 1.0 O A:GLY46 4.7 31.6 1.0 C A:GLY46 4.7 29.0 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of Friedel-Crafts Alkylating Enzyme Cylk From Cylindospermum Licheniforme with Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br711 b:15.9 occ:0.48 OD1 A:ASN334 2.5 12.7 0.5 O A:HOH1054 3.0 23.8 1.0 OG A:SER318 3.0 11.7 1.0 CG A:ASN334 3.4 11.2 0.5 O A:HOH1162 3.5 27.4 1.0 ND2 A:ASN334 3.5 14.6 0.5 N A:SER318 3.6 9.9 1.0 NE1 A:TRP320 3.6 9.2 1.0 CB A:SER318 3.7 11.6 1.0 C A:GLU317 3.8 9.5 1.0 CZ2 A:TRP320 3.9 9.1 1.0 CA A:GLU317 4.0 8.4 1.0 CG2 A:THR316 4.0 10.2 1.0 CE2 A:TRP320 4.1 8.6 1.0 CB A:ASN334 4.1 11.0 0.5 O A:ASN334 4.1 10.6 1.0 CA A:SER318 4.2 9.8 1.0 N A:GLU317 4.5 8.4 1.0 O A:HOH1198 4.5 22.2 1.0 O A:GLU317 4.5 9.7 1.0 NH1 A:ARG292 4.6 9.6 1.0 C A:ASN334 4.6 9.6 1.0 O A:THR316 4.7 10.2 1.0 C A:THR316 4.7 9.2 1.0 CB A:ASN334 4.8 11.5 0.5 CD1 A:TRP320 4.8 9.0 1.0 CA A:ASN334 4.8 10.5 0.5 O A:HOH1060 4.8 32.0 1.0 CD A:ARG292 4.9 8.9 1.0

N.R.Braffman, T.B.Ruskoski, K.M.Davis, N.R.Glasser, C.Johnson, C.D.Okafor, A.K.Boal, E.P.Balskus. Structural Basis For An Unprecedented Enzymatic Alkylation in Cylindrocyclophane Biosynthesis. Elife V. 11 2022.
ISSN: ESSN 2050-084X
PubMed: 35212625
DOI: 10.7554/ELIFE.75761