Bromine in PDB 7r3j: Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl

All present enzymatic activity of Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl:
3.1.2.32;

The structure of Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl, PDB code: 7r3j was solved by S.R.Borgert, S.Schmelz, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.47 / 3.06
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	159.256, 159.256, 284.1, 90, 90, 90
R / Rfree (%)	26.9 / 28.9

The structure of Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Bromine atom in the Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl (pdb code 7r3j). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl, PDB code: 7r3j:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl within 5.0Å range: probe atom residue distance (Å) B Occ C:Br700 b:141.5 occ:1.00 BR1 C:K5G700 0.0 141.5 1.0 C02 C:K5G700 1.9 73.4 1.0 C03 C:K5G700 2.8 69.2 1.0 C20 C:K5G700 2.8 75.9 1.0 H4 C:K5G700 3.0 92.7 1.0 H1 C:K5G700 3.0 84.6 1.0 HB2 C:LEU69 3.2 113.5 1.0 HD13 C:LEU69 3.2 111.4 1.0 HD22 C:LEU69 3.4 117.4 1.0 HB2 C:TYR64 3.4 91.9 1.0 H C:TYR64 3.5 90.9 1.0 H C:GLY62 3.5 89.2 1.0 HG13 C:VAL60 3.8 84.7 1.0 N C:GLY62 3.9 73.0 1.0 HA3 C:GLY62 3.9 78.9 1.0 HD2 C:TYR64 4.0 88.2 1.0 C C:GLY62 4.0 64.0 1.0 O C:HOH801 4.0 81.4 1.0 CB C:LEU69 4.1 93.2 1.0 O C:GLY62 4.1 69.2 1.0 C04 C:K5G700 4.1 69.0 1.0 C19 C:K5G700 4.1 71.1 1.0 CD1 C:LEU69 4.1 91.5 1.0 CA C:GLY62 4.2 64.4 1.0 N C:TYR64 4.2 74.4 1.0 CD2 C:LEU69 4.2 96.5 1.0 HA C:HIS61 4.3 87.7 1.0 CB C:TYR64 4.4 75.3 1.0 CG C:LEU69 4.4 95.9 1.0 N C:THR63 4.5 68.8 1.0 O C:TYR64 4.6 73.8 1.0 C C:HIS61 4.6 70.1 1.0 HG22 C:VAL60 4.6 81.3 1.0 HD11 C:LEU69 4.6 111.4 1.0 HA C:LEU69 4.6 110.0 1.0 HB3 C:LEU69 4.6 113.5 1.0 CD2 C:TYR64 4.7 72.2 1.0 C18 C:K5G700 4.7 73.8 1.0 CG1 C:VAL60 4.7 69.2 1.0 H C:THR63 4.7 84.2 1.0 HG11 C:VAL60 4.7 84.7 1.0 HD12 C:LEU69 4.7 111.4 1.0 HD21 C:LEU69 4.8 117.4 1.0 CA C:TYR64 4.8 71.9 1.0 HD23 C:LEU69 4.8 117.4 1.0 CA C:HIS61 4.9 71.8 1.0 CG C:TYR64 4.9 72.5 1.0 CA C:LEU69 4.9 90.3 1.0 H3 C:K5G700 5.0 86.9 1.0 HB3 C:TYR64 5.0 91.9 1.0

Bromine binding site 2 out of 2 in the Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Nativ Complex of Pqse and Rhlr with the Synthetic Antagonist Mbtl within 5.0Å range: probe atom residue distance (Å) B Occ D:Br700 b:233.0 occ:1.00 BR1 D:K5G700 0.0 233.0 1.0 C02 D:K5G700 1.9 143.0 1.0 H D:GLY62 2.7 153.1 1.0 C20 D:K5G700 2.8 147.6 1.0 C03 D:K5G700 2.8 148.6 1.0 H4 D:K5G700 2.9 178.7 1.0 H1 D:K5G700 3.0 179.9 1.0 N D:GLY62 3.0 126.2 1.0 C D:GLY62 3.2 117.8 1.0 O D:GLY62 3.3 125.3 1.0 HA3 D:GLY62 3.3 139.1 1.0 CA D:GLY62 3.4 114.5 1.0 H D:TYR64 3.5 143.6 1.0 HA D:HIS61 3.7 136.5 1.0 N D:THR63 3.8 117.2 1.0 HD22 D:LEU69 3.9 178.7 1.0 C D:HIS61 3.9 114.0 1.0 C19 D:K5G700 4.1 129.6 1.0 C04 D:K5G700 4.1 129.1 1.0 H D:THR63 4.2 142.2 1.0 HB2 D:TYR64 4.2 143.0 1.0 N D:TYR64 4.2 118.3 1.0 CA D:HIS61 4.3 112.4 1.0 HG23 D:VAL60 4.3 147.2 1.0 HA2 D:GLY62 4.3 139.1 1.0 HA D:THR63 4.4 141.7 1.0 HB2 D:LEU69 4.5 185.0 1.0 CA D:THR63 4.6 116.7 1.0 C18 D:K5G700 4.7 124.7 1.0 O D:HIS61 4.8 109.7 1.0 N D:HIS61 4.8 110.2 1.0 HD11 D:LEU69 4.8 179.7 1.0 O D:TYR64 4.8 124.4 1.0 CD2 D:LEU69 4.8 147.6 1.0 HD2 D:TYR64 4.9 138.2 1.0 C D:THR63 4.9 116.7 1.0 H3 D:K5G700 5.0 157.1 1.0

S.R.Borgert, S.Henke, F.Witzgall, S.Schmelz, S.Zur Lage, S.K.Hotop, S.Stephen, D.Lubken, J.Kruger, N.O.Gomez, M.Van Ham, L.Jansch, M.Kalesse, A.Pich, M.Bronstrup, S.Haussler, W.Blankenfeldt. Moonlighting Chaperone Activity of the Enzyme Pqse Contributes to Rhlr-Controlled Virulence of Pseudomonas Aeruginosa. Nat Commun V. 13 7402 2022.
ISSN: ESSN 2041-1723
PubMed: 36456567
DOI: 10.1038/S41467-022-35030-W