Manganese 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:

Fluorine	(F)	3 atoms
Chlorine	(Cl)	1 atom

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45, PDB code: 7ss6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Klebsiella Lpxh in Complex with Jh-Lph-45


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn 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:Mn301 b:26.9 occ:1.00 OD1 A:ASP8 2.0 23.9 1.0 O31 A:BKB303 2.1 29.8 1.0 NE2 A:HIS10 2.3 30.4 1.0 NE2 A:HIS197 2.3 26.8 1.0 OD2 A:ASP41 2.4 24.7 1.0 O A:HOH415 2.4 34.7 1.0 N30 A:BKB303 3.1 41.7 1.0 CE1 A:HIS10 3.1 31.6 1.0 CG A:ASP8 3.1 25.6 1.0 CE1 A:HIS197 3.1 31.2 1.0 CD2 A:HIS10 3.4 34.6 1.0 CG A:ASP41 3.4 28.4 1.0 MN A:MN302 3.4 27.1 1.0 CD2 A:HIS197 3.4 28.2 1.0 CB A:ASP41 3.6 20.2 1.0 CB A:ASP8 3.7 22.0 1.0 O29 A:BKB303 3.9 34.0 1.0 C28 A:BKB303 3.9 44.9 1.0 OD2 A:ASP8 4.1 26.0 1.0 CA A:ASP8 4.1 18.4 1.0 ND1 A:HIS10 4.3 33.7 1.0 ND1 A:HIS197 4.3 33.4 1.0 O A:HIS195 4.3 27.3 1.0 CG A:HIS10 4.4 25.3 1.0 CA A:HIS195 4.5 27.1 1.0 CG A:HIS197 4.5 27.1 1.0 OD1 A:ASP41 4.5 25.9 1.0 CE1 A:HIS114 4.5 23.4 1.0 NE2 A:HIS114 4.6 23.9 1.0 O A:HOH475 4.7 44.7 1.0 C A:HIS195 4.8 27.2 1.0 N A:HIS195 4.9 23.2 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn 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:Mn302 b:27.1 occ:1.00 OD1 A:ASN79 2.0 28.8 1.0 O31 A:BKB303 2.0 29.8 1.0 OD2 A:ASP41 2.2 24.7 1.0 NE2 A:HIS114 2.3 23.9 1.0 ND1 A:HIS195 2.3 26.0 1.0 O29 A:BKB303 2.7 34.0 1.0 N30 A:BKB303 2.9 41.7 1.0 CG A:ASN79 3.1 28.7 1.0 CG A:ASP41 3.1 28.4 1.0 CE1 A:HIS195 3.2 35.4 1.0 C28 A:BKB303 3.2 44.9 1.0 CE1 A:HIS114 3.2 23.4 1.0 CD2 A:HIS114 3.3 23.7 1.0 MN A:MN301 3.4 26.9 1.0 CG A:HIS195 3.4 23.2 1.0 OD1 A:ASP41 3.5 25.9 1.0 ND2 A:ASN79 3.7 30.5 1.0 CA A:HIS195 3.7 27.1 1.0 CB A:HIS195 3.8 23.7 1.0 O A:HOH415 3.9 34.7 1.0 OD1 A:ASP8 3.9 23.9 1.0 N A:ASN79 4.3 21.3 1.0 ND1 A:HIS114 4.3 23.3 1.0 NE2 A:HIS195 4.3 27.9 1.0 O A:HIS195 4.3 27.3 1.0 CB A:ASN79 4.4 26.1 1.0 CB A:ASP41 4.4 20.2 1.0 CG A:HIS114 4.4 21.7 1.0 CD2 A:HIS195 4.5 26.1 1.0 C A:HIS195 4.6 27.2 1.0 C27 A:BKB303 4.6 43.5 1.0 N A:HIS195 4.7 23.2 1.0 CA A:ASN79 4.9 22.9 1.0 CG A:ARG80 5.0 28.9 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