Fluorine in PDB 7ss6: Structure of Klebsiella Lpxh in Complex with Jh-Lph-45

All present enzymatic activity of Structure of Klebsiella Lpxh in Complex with Jh-Lph-45:
3.6.1.54;

The structure of Structure of Klebsiella Lpxh in Complex with Jh-Lph-45, PDB code: 7ss6 was solved by J.Cho, C.S.Cochrane, P.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.28 / 1.74
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	105.82, 105.82, 53.62, 90, 90, 120
R / Rfree (%)	16.7 / 19.5

The structure of Structure of Klebsiella Lpxh in Complex with Jh-Lph-45 also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Manganese	(Mn)	2 atoms

The binding sites of Fluorine atom in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45 (pdb code 7ss6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45, PDB code: 7ss6:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Klebsiella Lpxh in Complex with Jh-Lph-45 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:45.9 occ:1.00 F38 A:BKB303 0.0 45.9 1.0 C37 A:BKB303 1.4 35.3 1.0 F40 A:BKB303 2.2 46.5 1.0 F39 A:BKB303 2.2 52.7 1.0 C33 A:BKB303 2.3 33.1 1.0 C32 A:BKB303 2.8 31.4 1.0 C34 A:BKB303 3.4 29.6 1.0 SD A:MET156 3.7 41.9 1.0 C02 A:BKB303 4.1 26.0 1.0 CE A:MET156 4.4 41.1 1.0 C35 A:BKB303 4.6 28.5 1.0 C01 A:BKB303 4.9 26.3 1.0 CG2 A:ILE152 5.0 32.0 1.0 CE1 A:PHE128 5.0 53.3 1.0

Fluorine binding site 2 out of 3 in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Klebsiella Lpxh in Complex with Jh-Lph-45 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:52.7 occ:1.00 F39 A:BKB303 0.0 52.7 1.0 C37 A:BKB303 1.4 35.3 1.0 F40 A:BKB303 2.2 46.5 1.0 F38 A:BKB303 2.2 45.9 1.0 C33 A:BKB303 2.3 33.1 1.0 C34 A:BKB303 2.7 29.6 1.0 C32 A:BKB303 3.6 31.4 1.0 C35 A:BKB303 4.1 28.5 1.0 CG2 A:ILE137 4.6 38.2 1.0 C02 A:BKB303 4.7 26.0 1.0 CD1 A:PHE141 4.9 28.8 1.0 C01 A:BKB303 4.9 26.3 1.0

Fluorine binding site 3 out of 3 in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Klebsiella Lpxh in Complex with Jh-Lph-45 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:46.5 occ:1.00 F40 A:BKB303 0.0 46.5 1.0 C37 A:BKB303 1.4 35.3 1.0 F38 A:BKB303 2.2 45.9 1.0 F39 A:BKB303 2.2 52.7 1.0 C33 A:BKB303 2.4 33.1 1.0 C32 A:BKB303 2.9 31.4 1.0 C34 A:BKB303 3.4 29.6 1.0 CG2 A:ILE152 3.7 32.0 1.0 CD1 A:PHE141 4.0 28.8 1.0 CE1 A:PHE141 4.2 28.6 1.0 C02 A:BKB303 4.2 26.0 1.0 CD1 A:ILE152 4.5 33.0 1.0 SD A:MET156 4.5 41.9 1.0 C35 A:BKB303 4.6 28.5 1.0 C01 A:BKB303 4.9 26.3 1.0 CB A:ILE152 4.9 29.0 1.0

S.H.Kwaka, C.S.Cochrane, J.Cho, P.A.Dome, A.F.Ennis, J.H.Kim, P.Zhou, J.Hong. Development of Lpxh Inhibitors Chelating the Active Site Di-Manganese Metal Cluster of Lpxh Chemmedchem 2023.
ISSN: ESSN 1860-7187