Zinc in PDB 5v91: Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae

The structure of Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae, PDB code: 5v91 was solved by E.Klontz, S.Guenther, Z.Silverstein, E.Sundberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.69 / 1.30
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.875, 67.540, 89.508, 90.00, 90.00, 90.00
R / Rfree (%)	12.6 / 14.9

The binding sites of Zinc atom in the Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae (pdb code 5v91). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae, PDB code: 5v91:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:10.9 occ:1.00 OE1 A:GLU113 1.9 10.2 1.0 OE2 A:GLU98 1.9 11.7 1.0 NE2 A:HIS67 2.0 9.1 1.0 NE2 B:HIS7 2.0 9.1 1.0 CD A:GLU98 2.8 13.5 1.0 CD A:GLU113 2.9 10.6 1.0 CE1 B:HIS7 2.9 9.6 1.0 CD2 A:HIS67 3.0 8.8 1.0 HE1 B:HIS7 3.1 11.5 1.0 OE1 A:GLU98 3.1 14.8 1.0 CE1 A:HIS67 3.1 9.2 1.0 HD2 A:HIS67 3.1 10.5 1.0 CD2 B:HIS7 3.1 9.4 1.0 OE2 A:GLU113 3.1 11.8 1.0 HE1 A:TYR103 3.3 14.4 1.0 HE1 A:HIS67 3.3 11.0 1.0 HD2 B:HIS7 3.4 11.3 1.0 HB2 A:ALA69 3.5 11.2 1.0 HH A:TYR103 3.5 15.8 1.0 HG1 B:THR9 3.5 13.0 1.0 O A:HOH342 3.6 15.9 1.0 ND1 B:HIS7 4.1 9.3 1.0 OG1 B:THR9 4.1 10.8 1.0 CG A:HIS67 4.1 8.6 1.0 CE1 A:TYR103 4.1 12.0 1.0 ND1 A:HIS67 4.2 9.0 1.0 CG A:GLU98 4.2 14.0 1.0 CG B:HIS7 4.2 8.9 1.0 HG3 A:GLU98 4.3 16.8 1.0 CG A:GLU113 4.3 10.3 1.0 OH A:TYR103 4.3 13.1 1.0 CB A:ALA69 4.3 9.3 1.0 HB3 A:GLU113 4.4 11.5 1.0 HB2 A:GLU113 4.5 11.5 1.0 HB3 A:ALA69 4.5 11.2 1.0 HG2 A:GLU98 4.5 16.8 1.0 HG A:SER101 4.6 15.8 1.0 CB A:GLU113 4.6 9.6 1.0 HB1 A:ALA69 4.7 11.2 1.0 CZ A:TYR103 4.7 11.9 1.0 HH A:TYR65 4.7 23.8 1.0 HG3 A:GLU113 4.7 12.3 1.0 HB B:THR9 4.8 12.0 1.0 HG2 A:GLU113 4.8 12.3 1.0 HD1 B:HIS7 4.9 11.2 1.0 HD1 A:HIS67 4.9 10.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Fosfomycin Resistance Protein From Klebsiella Pneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:11.5 occ:0.76 OE1 B:GLU113 2.0 10.7 1.0 NE2 B:HIS67 2.1 10.2 1.0 NE2 A:HIS7 2.1 10.6 1.0 O B:HOH434 2.1 11.9 1.0 O A:HOH385 3.0 22.9 1.0 CD B:GLU113 3.0 10.7 1.0 CE1 A:HIS7 3.0 10.7 1.0 CD2 B:HIS67 3.0 9.6 1.0 CE1 B:HIS67 3.0 9.3 1.0 CD2 A:HIS7 3.1 10.3 1.0 HE1 A:HIS7 3.1 12.8 1.0 HD2 B:HIS67 3.2 11.5 1.0 HE1 B:HIS67 3.2 11.1 1.0 OE2 B:GLU113 3.3 12.1 1.0 HE1 B:TYR103 3.3 16.5 1.0 HD2 A:HIS7 3.3 12.3 1.0 HG1 A:THR9 3.4 12.5 1.0 HB2 B:ALA69 3.5 11.2 1.0 O B:HOH392 3.9 27.3 1.0 OG1 A:THR9 4.0 10.4 1.0 ND1 A:HIS7 4.2 9.6 1.0 ND1 B:HIS67 4.2 9.3 1.0 CE1 B:TYR103 4.2 13.8 1.0 CG B:HIS67 4.2 9.3 1.0 CG A:HIS7 4.2 9.7 1.0 HB3 B:GLU113 4.3 12.4 1.0 CG B:GLU113 4.3 10.4 1.0 CB B:ALA69 4.4 9.3 1.0 HB2 B:GLU113 4.5 12.4 1.0 OH B:TYR103 4.5 17.7 1.0 HB3 B:ALA69 4.6 11.2 1.0 HB A:THR9 4.6 11.4 1.0 CB B:GLU113 4.6 10.3 1.0 HB1 B:ALA69 4.7 11.2 1.0 CZ B:TYR103 4.8 14.6 1.0 HH B:TYR65 4.8 21.8 1.0 HG3 B:GLU113 4.8 12.5 1.0 CB A:THR9 4.9 9.5 1.0 HG2 B:GLU113 4.9 12.5 1.0 HD1 A:HIS7 4.9 11.5 1.0 HD1 B:HIS67 4.9 11.2 1.0

E.H.Klontz, A.D.Tomich, S.Gunther, J.A.Lemkul, D.Deredge, Z.Silverstein, J.F.Shaw, C.Mcelheny, Y.Doi, P.L.Wintrode, A.D.Mackerell, N.Sluis-Cremer, E.J.Sundberg. Structure and Dynamics of Fosa-Mediated Fosfomycin Resistance in Klebsiella Pneumoniae and Escherichia Coli. Antimicrob. Agents V. 61 2017CHEMOTHER..
ISSN: ESSN 1098-6596
PubMed: 28874374
DOI: 10.1128/AAC.01572-17