Manganese in PDB 6c3u: Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound

The structure of Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound, PDB code: 6c3u was solved by E.H.Klontz, E.J.Sundberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.53 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.765, 68.837, 90.312, 90.00, 90.46, 90.00
R / Rfree (%)	18.5 / 21.2

The structure of Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound also contains other interesting chemical elements:

Bromine

(Br)

4 atoms

The binding sites of Manganese atom in the Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound (pdb code 6c3u). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound, PDB code: 6c3u:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound


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 Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:18.4 occ:1.00 O16 A:NY2202 2.0 18.6 1.0 OE1 A:GLU113 2.1 12.2 1.0 NE2 A:HIS67 2.2 12.6 1.0 NE2 B:HIS7 2.3 12.9 1.0 O A:HOH335 2.4 17.9 1.0 C15 A:NY2202 3.0 20.7 1.0 CD A:GLU113 3.1 13.9 1.0 CD2 A:HIS67 3.1 16.4 1.0 CE1 A:HIS67 3.1 12.9 1.0 CE1 B:HIS7 3.2 13.9 1.0 CD2 B:HIS7 3.3 12.3 1.0 OE2 A:GLU113 3.4 13.1 1.0 OG1 B:THR9 3.7 12.4 1.0 N17 A:NY2202 3.9 21.6 1.0 C13 A:NY2202 3.9 20.2 1.0 CE1 A:TYR103 4.2 16.4 1.0 ND1 A:HIS67 4.3 11.9 1.0 CG A:HIS67 4.3 12.0 1.0 ND1 B:HIS7 4.4 9.0 1.0 BR A:NY2202 4.4 24.4 1.0 CB A:ALA69 4.4 10.7 1.0 CG A:GLU113 4.4 11.5 1.0 CG B:HIS7 4.4 11.5 1.0 OH A:TYR103 4.4 18.0 1.0 CB B:THR9 4.6 11.3 1.0 O A:HOH377 4.7 24.2 1.0 CB A:GLU113 4.7 10.6 1.0 OH A:TYR65 4.7 17.6 1.0 CZ A:TYR103 4.8 16.9 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound


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 Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:18.4 occ:1.00 O16 A:NY2203 2.1 21.6 1.0 OE1 B:GLU113 2.1 13.2 1.0 NE2 A:HIS7 2.2 13.3 1.0 NE2 B:HIS67 2.2 15.6 1.0 O B:HOH323 2.3 19.4 1.0 C15 A:NY2203 3.0 21.8 1.0 CD B:GLU113 3.1 14.7 1.0 CE1 A:HIS7 3.1 14.3 1.0 CD2 B:HIS67 3.2 14.9 1.0 CE1 B:HIS67 3.2 17.0 1.0 CD2 A:HIS7 3.2 16.2 1.0 OE2 B:GLU113 3.4 17.8 1.0 OG1 A:THR9 3.7 14.3 1.0 C13 A:NY2203 3.8 22.7 1.0 N17 A:NY2203 3.9 26.6 1.0 BR A:NY2203 4.2 26.9 1.0 CE1 B:TYR103 4.3 18.6 1.0 ND1 A:HIS7 4.3 15.7 1.0 ND1 B:HIS67 4.3 12.8 1.0 CG B:HIS67 4.3 14.1 1.0 OH B:TYR103 4.4 27.2 1.0 CG A:HIS7 4.4 14.0 1.0 CB B:ALA69 4.4 16.0 1.0 CG B:GLU113 4.5 16.5 1.0 O B:HOH318 4.6 28.1 1.0 CB A:THR9 4.7 13.7 1.0 OH B:TYR65 4.8 19.0 1.0 CB B:GLU113 4.8 15.4 1.0 CZ B:TYR103 4.8 23.8 1.0 C12 A:NY2203 5.0 24.3 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn201 b:19.3 occ:1.00 O16 D:NY2203 2.1 19.3 1.0 OE1 C:GLU113 2.1 15.2 1.0 O C:HOH369 2.2 18.8 1.0 NE2 D:HIS7 2.3 15.2 1.0 NE2 C:HIS67 2.3 16.9 1.0 C15 D:NY2203 3.0 21.4 1.0 CD C:GLU113 3.1 18.3 1.0 CD2 C:HIS67 3.2 14.5 1.0 CE1 D:HIS7 3.2 18.3 1.0 CD2 D:HIS7 3.3 18.0 1.0 CE1 C:HIS67 3.3 16.0 1.0 OE2 C:GLU113 3.4 16.5 1.0 OG1 D:THR9 3.7 14.8 1.0 C13 D:NY2203 3.9 21.3 1.0 N17 D:NY2203 4.0 22.2 1.0 BR D:NY2203 4.3 23.4 1.0 ND1 D:HIS7 4.3 19.2 1.0 CE1 C:TYR103 4.3 19.9 1.0 CG C:HIS67 4.4 15.6 1.0 ND1 C:HIS67 4.4 17.2 1.0 CG D:HIS7 4.4 15.2 1.0 CB C:ALA69 4.4 13.3 1.0 CG C:GLU113 4.4 15.9 1.0 O C:HOH365 4.6 28.4 1.0 CB D:THR9 4.6 16.0 1.0 OH C:TYR103 4.6 23.4 1.0 CB C:GLU113 4.7 15.8 1.0 OH C:TYR65 4.9 18.1 1.0 CZ C:TYR103 5.0 22.6 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Klebsiella Pneumoniae Fosfomycin Resistance Protein (Fosakp) with Inhibitor (ANY2) Bound within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn201 b:16.8 occ:1.00 O16 D:NY2202 2.0 23.0 1.0 OE1 D:GLU113 2.1 12.9 1.0 NE2 D:HIS67 2.2 12.6 1.0 NE2 C:HIS7 2.2 12.2 1.0 O D:HOH313 2.3 19.7 1.0 C15 D:NY2202 3.0 17.7 1.0 CD D:GLU113 3.1 18.1 1.0 CD2 D:HIS67 3.2 12.2 1.0 CE1 C:HIS7 3.2 13.8 1.0 CD2 C:HIS7 3.2 15.3 1.0 CE1 D:HIS67 3.2 16.2 1.0 OE2 D:GLU113 3.4 13.3 1.0 OG1 C:THR9 3.7 13.4 1.0 C13 D:NY2202 3.8 16.2 1.0 N17 D:NY2202 3.9 24.0 1.0 CE1 D:TYR103 4.2 19.1 1.0 BR D:NY2202 4.2 22.9 1.0 OH D:TYR103 4.3 21.1 1.0 ND1 C:HIS7 4.3 15.1 1.0 ND1 D:HIS67 4.3 14.0 1.0 CG D:HIS67 4.3 12.5 1.0 CG C:HIS7 4.4 17.2 1.0 CG D:GLU113 4.5 13.3 1.0 CB D:ALA69 4.5 14.7 1.0 CB C:THR9 4.6 15.4 1.0 CZ D:TYR103 4.7 21.9 1.0 O D:HOH386 4.7 28.6 1.0 CB D:GLU113 4.8 16.8 1.0 OH D:TYR65 4.9 23.4 1.0 C12 D:NY2202 5.0 22.6 1.0 N18 D:NY2202 5.0 24.0 1.0

A.D.Tomich, E.H.Klontz, D.Deredge, J.P.Barnard, C.L.Mcelheny, M.L.Eshbach, O.A.Weisz, P.Wintrode, Y.Doi, E.J.Sundberg, N.Sluis-Cremer. Small-Molecule Inhibitor of Fosa Expands Fosfomycin Activity to Multidrug-Resistant Gram-Negative Pathogens. Antimicrob. Agents V. 63 2019CHEMOTHER..
ISSN: ESSN 1098-6596
PubMed: 30642934
DOI: 10.1128/AAC.01524-18