Zinc in PDB 3f9o: Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila

All present enzymatic activity of Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila:
3.5.2.6;

The structure of Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila, PDB code: 3f9o was solved by H.Delbruck, K.M.V.Hoffmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.56 / 2.03
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	42.800, 101.050, 116.490, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 20.2

The structure of Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila also contains other interesting chemical elements:

Chlorine

(Cl)

6 atoms

The binding sites of Zinc atom in the Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila (pdb code 3f9o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila, PDB code: 3f9o:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila


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 the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn308 b:17.5 occ:1.00 OD2 A:ASP120 2.0 12.6 1.0 O3 A:SO41 2.0 18.2 1.0 NE2 A:HIS263 2.1 12.4 1.0 SG A:CYS221 2.3 14.0 1.0 CG A:ASP120 3.0 10.2 1.0 CE1 A:HIS263 3.0 12.2 1.0 CD2 A:HIS263 3.1 12.3 1.0 O A:HOH474 3.1 15.7 1.0 S A:SO41 3.2 9.2 1.0 CB A:CYS221 3.3 14.0 1.0 OD1 A:ASP120 3.4 10.8 1.0 O2 A:SO41 3.5 22.1 1.0 O A:HOH107 3.7 26.2 1.0 O4 A:SO41 3.7 18.0 1.0 NH2 A:ARG121 3.9 14.1 1.0 ZN A:ZN309 4.1 19.6 1.0 ND1 A:HIS263 4.2 10.1 1.0 CA A:CYS221 4.2 14.0 1.0 CG A:HIS263 4.2 10.6 1.0 CB A:ASP120 4.3 10.3 1.0 O1 A:SO41 4.4 24.1 1.0 CZ A:ARG121 4.4 13.2 1.0 NE A:ARG121 4.5 12.7 1.0 NE2 A:HIS196 4.5 12.6 1.0 CD2 A:HIS196 4.9 13.1 1.0 O A:HOH334 4.9 21.7 1.0 N A:CYS221 4.9 14.4 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila


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 the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn309 b:19.6 occ:1.00 O4 A:SO41 1.9 18.0 1.0 O A:HOH474 2.0 15.7 1.0 ND1 A:HIS118 2.0 12.2 1.0 NE2 A:HIS196 2.0 12.6 1.0 CE1 A:HIS118 2.9 13.2 1.0 CE1 A:HIS196 3.0 12.9 1.0 S A:SO41 3.0 9.2 1.0 CD2 A:HIS196 3.1 13.1 1.0 CG A:HIS118 3.1 11.1 1.0 O3 A:SO41 3.2 18.2 1.0 CB A:HIS118 3.5 10.8 1.0 O1 A:SO41 3.7 24.1 1.0 O A:HOH334 3.8 21.7 1.0 NE2 A:HIS118 4.0 12.1 1.0 ZN A:ZN308 4.1 17.5 1.0 ND1 A:HIS196 4.1 13.5 1.0 OD1 A:ASP120 4.1 10.8 1.0 CD2 A:HIS118 4.2 12.9 1.0 CG A:HIS196 4.2 12.7 1.0 O2 A:SO41 4.2 22.1 1.0 SG A:CYS221 4.4 14.0 1.0 CG2 A:THR197 4.5 13.0 1.0 OD2 A:ASP120 4.6 12.6 1.0 ND2 A:ASN116 4.7 11.7 1.0 CG A:ASP120 4.7 10.2 1.0 CB A:CYS221 4.8 14.0 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Di-Zinc Carbapenemase Cpha From Aeromonas Hydrophila within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn310 b:20.9 occ:0.75 ND1 A:HIS289 2.1 12.8 1.0 CL A:CL12 2.2 41.7 1.0 CL A:CL11 2.2 34.7 1.0 CE1 A:HIS289 3.1 12.6 1.0 CG A:HIS289 3.1 10.9 1.0 CL A:CL10 3.2 30.5 1.0 CB A:HIS289 3.4 10.9 1.0 CA A:HIS289 4.1 10.6 1.0 NE2 A:HIS289 4.2 11.6 1.0 CD2 A:HIS289 4.2 10.6 1.0 N A:GLY290 4.5 10.9 1.0 CD1 A:LEU293 4.6 11.2 1.0 C A:HIS289 4.9 10.7 1.0 O A:LEU267 4.9 10.8 1.0 N A:LEU293 5.0 10.6 1.0

C.Bebrone, H.Delbruck, M.B.Kupper, P.Schlomer, C.Willmann, J.-M.Frere, R.Fischer, M.Galleni, K.M.V.Hoffmann. The Structure of the Dizinc Subclass B2 Metallo-Beta-Lactamase Cpha Reveals That the Second Inhibitory Zinc Ion Binds in the Histidine Site Antimicrob.Agents Chemother. V. 53 4464 2009.
ISSN: ISSN 0066-4804
PubMed: 19651913
DOI: 10.1128/AAC.00288-09