Zinc in PDB 3iof: Crystal Structure of Cpha N220G Mutant with Inhibitor 10A

All present enzymatic activity of Crystal Structure of Cpha N220G Mutant with Inhibitor 10A:
3.5.2.6;

The structure of Crystal Structure of Cpha N220G Mutant with Inhibitor 10A, PDB code: 3iof was solved by H.Delbruck, C.Bebrone, K.M.V.Hoffmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.59 / 1.44
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	42.650, 100.660, 116.990, 90.00, 90.00, 90.00
R / Rfree (%)	12.3 / 14.1

The binding sites of Zinc atom in the Crystal Structure of Cpha N220G Mutant with Inhibitor 10A (pdb code 3iof). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Cpha N220G Mutant with Inhibitor 10A, PDB code: 3iof:

Zinc binding site 1 out of 1 in the Crystal Structure of Cpha N220G Mutant with Inhibitor 10A


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 Cpha N220G Mutant with Inhibitor 10A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:8.1 occ:0.80 OD2 A:ASP120 2.0 9.3 1.0 NE2 A:HIS263 2.1 8.0 1.0 S1 A:IFS308 2.3 9.9 0.8 SG A:CYS221 2.3 9.8 1.0 CG A:ASP120 3.0 7.6 1.0 CE1 A:HIS263 3.0 9.7 1.0 C7 A:IFS308 3.2 14.8 0.8 CD2 A:HIS263 3.2 7.9 1.0 OD1 A:ASP120 3.2 8.6 1.0 CB A:CYS221 3.3 9.8 1.0 NH2 A:ARG121 3.9 7.4 1.0 ND1 A:HIS263 4.2 8.1 1.0 CA A:CYS221 4.2 8.2 1.0 CB A:ASP120 4.3 6.7 1.0 CG A:HIS263 4.3 7.9 1.0 C102 A:IFS308 4.4 16.8 0.8 CE1 A:HIS196 4.5 10.4 1.0 NE A:ARG121 4.5 5.2 1.0 NE2 A:HIS196 4.5 10.3 1.0 CZ A:ARG121 4.5 5.3 1.0 O A:HOH333 4.6 9.0 1.0 C2 A:IFS308 4.6 17.9 0.8 O A:HOH435 4.7 10.9 1.0 N A:CYS221 4.9 7.9 1.0

P.Lassaux, M.Hamel, M.Gulea, H.Delbruck, P.S.Mercuri, L.Horsfall, D.Dehareng, M.Kupper, J.-M.Frere, K.Hoffmann, M.Galleni, C.Bebrone. Mercaptophosphonate Compounds As Broad-Spectrum Inhibitors of the Metallo-Beta-Lactamases J.Med.Chem. V. 53 4862 2010.
ISSN: ISSN 0022-2623
PubMed: 20527888
DOI: 10.1021/JM100213C