Zinc in PDB 6dr8: Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H

The structure of Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H, PDB code: 6dr8 was solved by M.Monteiro Pedroso, D.Waite, M.Natasa, R.Mcgeary, L.Guddat, P.Hugenholtz, G.Schenk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.58 / 1.48
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.767, 69.151, 77.523, 90.00, 90.00, 90.00
R / Rfree (%)	13.2 / 16.7

The binding sites of Zinc atom in the Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H (pdb code 6dr8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H, PDB code: 6dr8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn405 b:32.6 occ:0.45 O3 A:PO4402 1.9 15.3 0.6 O1 A:PO4402 2.0 26.8 0.4 NE2 A:HIS121 2.1 11.7 1.0 O1 A:PO4402 2.1 29.6 0.6 O3 A:PO4402 2.2 16.1 0.4 OD2 A:ASP120 2.2 19.7 0.8 P A:PO4402 2.3 11.3 0.6 P A:PO4402 2.4 34.0 0.4 NE2 A:HIS254 2.5 22.7 0.5 HD2 A:HIS254 2.6 26.8 0.5 CE1 A:HIS121 2.7 11.0 1.0 HE1 A:HIS121 2.8 13.2 1.0 CD2 A:HIS254 2.8 22.4 0.5 O2 A:PO4402 3.0 17.7 0.6 CG A:ASP120 3.0 18.0 1.0 CD2 A:HIS121 3.1 11.5 1.0 O2 A:PO4402 3.1 17.0 0.4 OD1 A:ASP120 3.3 17.8 0.8 HH12 A:ARG257 3.4 21.5 1.0 HD2 A:HIS121 3.5 13.8 1.0 O4 A:PO4402 3.7 12.4 0.6 CE1 A:HIS254 3.7 23.4 0.5 O4 A:PO4402 3.8 28.5 0.4 ND1 A:HIS121 3.8 10.0 1.0 HE1 A:HIS116 3.8 8.2 1.0 CG A:HIS121 4.0 8.9 1.0 HE1 A:HIS254 4.1 28.1 0.5 CG A:HIS254 4.2 20.5 0.5 NH1 A:ARG257 4.2 17.9 1.0 O A:HOH501 4.2 35.5 1.0 HB2 A:ASP120 4.2 18.2 1.0 CB A:ASP120 4.3 15.2 1.0 HH22 A:ARG257 4.3 20.3 1.0 HD2 A:HIS254 4.4 23.6 0.5 HD22 A:LEU70 4.4 27.3 1.0 CE1 A:HIS116 4.4 6.9 1.0 HB2 A:HIS254 4.5 17.6 0.5 ZN A:ZN406 4.5 9.0 1.0 HD1 A:HIS121 4.5 12.0 1.0 ND1 A:HIS254 4.5 23.4 0.5 HH11 A:ARG257 4.5 21.5 1.0 NE2 A:HIS116 4.6 7.3 1.0 O A:HOH583 4.7 38.5 1.0 HB2 A:SER214 4.8 13.1 1.0 HD21 A:ASN253 4.9 12.2 1.0 HB3 A:ASP120 4.9 18.2 1.0 NH2 A:ARG257 4.9 16.9 1.0 ND2 A:ASN253 5.0 10.2 1.0 O A:ASN253 5.0 11.2 1.0 OD1 A:ASN253 5.0 10.8 1.0 CZ A:ARG257 5.0 17.4 1.0 HB2 A:HIS118 5.0 8.6 1.0

Zinc binding site 2 out of 2 in the Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo-Beta-Lactamase From Cronobacter Sakazakii (Enterobacter Sakazakii) Harldq Motif Mutant S60/R118H/Q121H/K254H within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn406 b:9.0 occ:1.00 O2 A:PO4402 1.9 17.7 0.6 O2 A:PO4402 2.0 17.0 0.4 ND1 A:HIS118 2.0 7.8 1.0 NE2 A:HIS116 2.0 7.3 1.0 NE2 A:HIS192 2.0 7.1 1.0 CE1 A:HIS118 2.9 8.6 1.0 CE1 A:HIS116 2.9 6.9 1.0 CE1 A:HIS192 3.0 7.6 1.0 CD2 A:HIS116 3.0 6.9 1.0 HE1 A:HIS118 3.0 10.3 1.0 CD2 A:HIS192 3.0 7.2 1.0 CG A:HIS118 3.1 6.9 1.0 HB2 A:HIS118 3.1 8.6 1.0 HE1 A:HIS116 3.1 8.2 1.0 P A:PO4402 3.1 11.3 0.6 P A:PO4402 3.2 34.0 0.4 HE1 A:HIS192 3.2 9.1 1.0 HD2 A:HIS192 3.2 8.6 1.0 HD2 A:HIS116 3.2 8.3 1.0 O3 A:PO4402 3.4 16.1 0.4 CB A:HIS118 3.5 7.1 1.0 O3 A:PO4402 3.6 15.3 0.6 O4 A:PO4402 3.7 12.4 0.6 HB3 A:HIS118 3.7 8.6 1.0 O A:HOH583 3.8 38.5 1.0 O4 A:PO4402 3.8 28.5 0.4 HD2 A:HIS121 3.9 13.8 1.0 ND1 A:HIS116 4.0 7.7 1.0 NE2 A:HIS118 4.0 9.7 1.0 CG A:HIS116 4.1 7.8 1.0 ND1 A:HIS192 4.1 7.3 1.0 CD2 A:HIS118 4.1 8.6 1.0 CG A:HIS192 4.2 6.8 1.0 O1 A:PO4402 4.3 29.6 0.6 O1 A:PO4402 4.3 26.8 0.4 ZN A:ZN405 4.5 32.6 0.5 HG A:SER214 4.5 15.7 1.0 CD2 A:HIS121 4.6 11.5 1.0 HB3 A:SER214 4.6 13.1 1.0 OD1 A:ASP120 4.6 17.8 0.8 HG A:LEU193 4.6 11.4 1.0 NE2 A:HIS121 4.7 11.7 1.0 HD1 A:HIS116 4.7 9.3 1.0 HE2 A:HIS118 4.8 11.6 1.0 HB2 A:SER214 4.8 13.1 1.0 HD1 A:HIS192 4.9 8.7 1.0 CA A:HIS118 4.9 6.9 1.0 HD11 A:LEU193 5.0 10.3 1.0

M.Monteiro Pedroso, D.Waite, M.Natasa, R.Mcgeary, L.Guddat, P.Hugenholtz, G.Schenk. Evolution and Diversity of B3-Type Metallo-Beta-Lactamases, Emerging Contributors to the Spread of Antibiotic Resistance. To Be Published.