Manganese in PDB 7ss7: Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50

All present enzymatic activity of Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50:
3.6.1.54;

The structure of Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50, PDB code: 7ss7 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)	46.32 / 1.73
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.53, 106.53, 53.56, 90, 90, 120
R / Rfree (%)	16.8 / 19.3

The structure of Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50 also contains other interesting chemical elements:

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

The binding sites of Manganese atom in the Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50 (pdb code 7ss7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50, PDB code: 7ss7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:23.2 occ:1.00 OD1 A:ASP8 2.1 18.6 1.0 O30 A:BN8303 2.1 25.9 1.0 NE2 A:HIS10 2.3 21.6 1.0 NE2 A:HIS197 2.4 23.1 1.0 OD2 A:ASP41 2.4 21.7 1.0 O28 A:BN8303 2.5 28.9 1.0 N29 A:BN8303 3.0 57.3 1.0 CE1 A:HIS10 3.1 27.1 1.0 CG A:ASP8 3.1 19.9 1.0 C27 A:BN8303 3.1 50.1 1.0 CE1 A:HIS197 3.2 28.7 1.0 CD2 A:HIS10 3.4 26.1 1.0 MN A:MN302 3.4 25.6 1.0 CG A:ASP41 3.4 22.5 1.0 CD2 A:HIS197 3.5 23.5 1.0 CB A:ASP41 3.6 16.4 1.0 CB A:ASP8 3.7 16.9 1.0 OD2 A:ASP8 4.1 22.0 1.0 CA A:ASP8 4.1 14.4 1.0 ND1 A:HIS10 4.3 28.9 1.0 ND1 A:HIS197 4.3 28.7 1.0 O A:HIS195 4.4 22.4 1.0 CG A:HIS10 4.4 21.4 1.0 CG A:HIS197 4.5 22.5 1.0 CE1 A:HIS114 4.5 17.9 1.0 CA A:HIS195 4.5 20.2 1.0 OD1 A:ASP41 4.5 18.0 1.0 C26 A:BN8303 4.7 49.8 1.0 NE2 A:HIS114 4.7 16.8 1.0 O A:HOH440 4.8 38.7 1.0 C A:HIS195 4.9 20.2 1.0 OD1 A:ASN79 5.0 25.0 1.0 N A:HIS195 5.0 17.6 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Klebsiella Lpxh in Complex with Jh-Lph-50 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:25.6 occ:1.00 OD1 A:ASN79 1.9 25.0 1.0 O30 A:BN8303 2.1 25.9 1.0 NE2 A:HIS114 2.3 16.8 1.0 ND1 A:HIS195 2.3 23.6 1.0 OD2 A:ASP41 2.3 21.7 1.0 N29 A:BN8303 2.4 57.3 1.0 CE1 A:HIS195 3.1 30.4 1.0 CG A:ASN79 3.1 24.4 1.0 CE1 A:HIS114 3.1 17.9 1.0 CG A:ASP41 3.2 22.5 1.0 C27 A:BN8303 3.3 50.1 1.0 CD2 A:HIS114 3.4 16.6 1.0 MN A:MN301 3.4 23.2 1.0 CG A:HIS195 3.4 20.3 1.0 ND2 A:ASN79 3.7 27.9 1.0 OD1 A:ASP41 3.7 18.0 1.0 CA A:HIS195 3.8 20.2 1.0 O28 A:BN8303 3.8 28.9 1.0 CB A:HIS195 3.9 18.0 1.0 OD1 A:ASP8 3.9 18.6 1.0 N A:ASN79 4.2 16.6 1.0 NE2 A:HIS195 4.3 26.4 1.0 ND1 A:HIS114 4.3 16.9 1.0 CB A:ASN79 4.3 22.0 1.0 O A:HIS195 4.3 22.4 1.0 C26 A:BN8303 4.4 49.8 1.0 CG A:HIS114 4.4 16.7 1.0 CB A:ASP41 4.5 16.4 1.0 CD2 A:HIS195 4.5 22.6 1.0 C A:HIS195 4.6 20.2 1.0 N A:HIS195 4.7 17.6 1.0 CA A:ASN79 4.8 18.1 1.0 C25 A:BN8303 5.0 46.6 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