Zinc in PDB 3fai: The Di Zinc Carbapenemase Cpha N220G Mutant

All present enzymatic activity of The Di Zinc Carbapenemase Cpha N220G Mutant:
3.5.2.6;

The structure of The Di Zinc Carbapenemase Cpha N220G Mutant, PDB code: 3fai 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)	19.60 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	42.680, 101.060, 116.820, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16

The structure of The Di Zinc Carbapenemase Cpha N220G Mutant also contains other interesting chemical elements:

Chlorine

(Cl)

7 atoms

The binding sites of Zinc atom in the The Di Zinc Carbapenemase Cpha N220G Mutant (pdb code 3fai). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the The Di Zinc Carbapenemase Cpha N220G Mutant, PDB code: 3fai:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the The Di Zinc Carbapenemase Cpha N220G Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Di Zinc Carbapenemase Cpha N220G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:10.5 occ:1.00 OD2 A:ASP120 2.0 5.0 1.0 NE2 A:HIS263 2.0 3.7 1.0 O1 A:SO4311 2.1 8.5 0.5 O A:HOH227 2.3 2.0 0.5 SG A:CYS221 2.3 2.0 1.0 CE1 A:HIS263 3.0 2.9 1.0 CG A:ASP120 3.0 5.3 1.0 CD2 A:HIS263 3.1 5.6 1.0 S A:SO4311 3.2 2.1 0.5 O A:HOH519 3.3 6.2 1.0 CB A:CYS221 3.3 2.7 1.0 OD1 A:ASP120 3.4 8.4 1.0 O4 A:SO4311 3.5 18.5 0.5 O2 A:SO4311 3.8 9.1 0.5 NH2 A:ARG121 3.8 4.4 1.0 CA A:CYS221 4.1 2.0 1.0 ND1 A:HIS263 4.1 2.9 1.0 CG A:HIS263 4.2 4.0 1.0 ZN A:ZN2 4.2 9.8 0.8 CB A:ASP120 4.3 3.0 1.0 O3 A:SO4311 4.4 20.1 0.5 NE2 A:HIS196 4.5 7.8 1.0 CZ A:ARG121 4.5 5.2 1.0 NE A:ARG121 4.6 2.7 1.0 N A:CYS221 4.8 2.0 1.0 O A:HOH363 4.9 12.3 1.0 CD2 A:HIS196 5.0 6.9 1.0 CE1 A:HIS196 5.0 13.4 1.0

Zinc binding site 2 out of 3 in the The Di Zinc Carbapenemase Cpha N220G Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Di Zinc Carbapenemase Cpha N220G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:9.8 occ:0.80 ND1 A:HIS118 2.0 8.5 1.0 O A:HOH519 2.0 6.2 1.0 NE2 A:HIS196 2.0 7.8 1.0 O2 A:SO4311 2.1 9.1 0.5 O A:HOH464 2.5 22.8 1.0 CE1 A:HIS118 2.9 7.8 1.0 CE1 A:HIS196 3.0 13.4 1.0 CD2 A:HIS196 3.1 6.9 1.0 CG A:HIS118 3.1 5.7 1.0 S A:SO4311 3.2 2.1 0.5 O1 A:SO4311 3.3 8.5 0.5 CB A:HIS118 3.6 2.8 1.0 O3 A:SO4311 3.7 20.1 0.5 O A:HOH227 3.7 2.0 0.5 O A:HOH363 3.8 12.3 1.0 NE2 A:HIS118 4.0 7.8 1.0 ND1 A:HIS196 4.1 11.6 1.0 CD2 A:HIS118 4.2 7.3 1.0 OD1 A:ASP120 4.2 8.4 1.0 CG A:HIS196 4.2 9.2 1.0 ZN A:ZN1 4.2 10.5 1.0 O4 A:SO4311 4.4 18.5 0.5 O A:HOH499 4.5 34.2 1.0 SG A:CYS221 4.5 2.0 1.0 CG2 A:THR197 4.6 10.2 1.0 ND2 A:ASN116 4.6 4.7 1.0 OD2 A:ASP120 4.7 5.0 1.0 CG A:ASP120 4.8 5.3 1.0 CB A:CYS221 5.0 2.7 1.0

Zinc binding site 3 out of 3 in the The Di Zinc Carbapenemase Cpha N220G Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Di Zinc Carbapenemase Cpha N220G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3 b:16.8 occ:0.50 ND1 A:HIS289 2.1 7.8 1.0 O A:HOH518 2.2 8.3 0.5 CL A:CL310 2.2 25.8 0.5 CL A:CL309 2.4 22.2 0.5 OE2 A:GLU292 2.5 14.1 0.5 CE1 A:HIS289 3.0 8.4 1.0 CL A:CL308 3.2 15.5 0.5 CG A:HIS289 3.2 5.5 1.0 CB A:HIS289 3.6 5.3 1.0 CD A:GLU292 3.6 11.9 0.5 CG A:GLU292 4.0 9.2 0.5 CA A:HIS289 4.1 2.5 1.0 NE2 A:HIS289 4.2 7.4 1.0 CD2 A:HIS289 4.3 5.7 1.0 N A:GLY290 4.5 5.8 1.0 CD1 A:LEU293 4.7 5.3 1.0 OE1 A:GLU292 4.7 12.2 0.5 C A:HIS289 4.9 6.4 1.0 O A:LEU267 4.9 5.9 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