Mercury in the structure of Carbonic Anhydrase Activators. Activation Of Isozymes I, II, IV, Va, VII And Xiv With L- And D-Histidine and Crystallographic Analysis Of Their Adducts With Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme (pdb 2ez7)

The binding sites of Mercury atom in the structure of Carbonic Anhydrase Activators. Activation Of Isozymes I, II, IV, Va, VII And Xiv With L- And D-Histidine and Crystallographic Analysis Of Their Adducts With Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme (pdb code 2ez7). This binding sites where shown with 5.0 Angstroms radius around Mercury atom. The 2ez7 structure was solved by C.TEMPERINI, A.SCOZZAFAVA, D.VULLO, C.T.SUPURAN, with X-Ray Crystallography technique, brief refinement statistics is given in the table below: Resolution (A) 8.0-2.0 Space group P1211 a (A) 42.060 b (A) 41.430 c (A) 72.520 alpha (°) 90.00 beta (°) 104.40 gamma (°) 90.00 Rfactor (%) 24.9 Rfree (%) 30 Mercury Binding Sites: Mercury binding site 1 out of 1 in 2ez7 Click to enlarge Click to enlarge Mono- and Stereo- picture of 5.0 Angstrom coordination sphere 1 of Mercury in the PDB 2ez7. Coordination sphere was calculated for all residues within 5.0 Angstroms distance from the central Mercury atom, shown by VdW sphere Residues shown as a stick model or VDW spheres: A: Val135, A: Gln136, A: Gln137, A: Pro138, A: Leu204, A: Glu205, A: Cys206, A: Hoh485, A: Hoh529, conact list: Atom Atom Distance (A) Hg O A:Val135 4.22 Hg C A:Val135 4.49 Hg O A:Gln136 4.96 Hg N A:Gln136 4.69 Hg C A:Gln136 4.29 Hg CA A:Gln136 4.64 Hg O A:Gln137 2.97 Hg N A:Gln137 3.77 Hg C A:Gln137 3.45 Hg CA A:Gln137 4.13 Hg N A:Pro138 4.08 Hg CA A:Pro138 4.30 Hg C A:Leu204 5.00 Hg O A:Glu205 2.93 Hg N A:Glu205 4.48 Hg C A:Glu205 3.42 Hg CA A:Glu205 4.52 Hg N A:Cys206 3.66 Hg CB A:Cys206 3.04 Hg SG A:Cys206 4.04 Hg C A:Cys206 4.85 Hg CA A:Cys206 3.39 Hg O A:Hoh485 2.65 Hg O A:Hoh529 2.93 interactive model: