Magnesium in the structure of Rat Catechol O-Methyltransferase in Complex With A Bisubstrate Inhibitor (pdb 3hvi)

The binding sites of Magnesium atom in the structure of Rat Catechol O-Methyltransferase in Complex With A Bisubstrate Inhibitor (pdb code 3hvi). This binding sites where shown with 5.0 Angstroms radius around Magnesium atom. The 3hvi structure was solved by A.EHLER, D.SCHLATTER, M.STIHLE, J.BENZ, M.G.RUDOLPH, with X-Ray Crystallography technique, brief refinement statistics is given in the table below: Resolution (A) 32.5-1.2 Space group P212121 a (A) 49.857 b (A) 54.706 c (A) 80.617 alpha (°) 90.00 beta (°) 90.00 gamma (°) 90.00 Rfactor (%) 13.1 Rfree (%) 16.1 Magnesium Binding Sites: Magnesium binding site 1 out of 1 in 3hvi Click to enlarge Click to enlarge Mono- and Stereo- picture of 5.0 Angstrom coordination sphere 1 of Magnesium in the PDB 3hvi. Coordination sphere was calculated for all residues within 5.0 Angstroms distance from the central Magnesium atom, shown by VdW sphere Residues shown as a stick model or VDW spheres: A: Met83, A: Lys89, A: Asp184, A: Lys187, A: Asp212, A: Asn213, A: Glu242, A: 619267, A: Hoh334, A: Hoh371, A: Hoh445, conact list: Atom Atom Distance (A) Mg O A:Met83 4.30 Mg NZ A:Lys89 4.75 Mg O A:Asp184 4.76 Mg CB A:Asp184 4.41 Mg OD2 A:Asp184 3.38 Mg OD1 A:Asp184 2.08 Mg CG A:Asp184 3.04 Mg CA A:Asp184 4.87 Mg CE A:Lys187 4.66 Mg NZ A:Lys187 3.78 Mg CB A:Asp212 3.76 Mg OD2 A:Asp212 2.07 Mg OD1 A:Asp212 4.13 Mg CG A:Asp212 3.15 Mg CB A:Asn213 4.48 Mg ND2 A:Asn213 3.40 Mg OD1 A:Asn213 2.15 Mg CG A:Asn213 3.11 Mg OE1 A:Glu242 4.80 Mg OE2 A:Glu242 4.20 Mg CD A:Glu242 4.87 Mg O32 A:619267 2.14 Mg C31 A:619267 2.91 Mg O34 A:619267 2.07 Mg C20 A:619267 4.27 Mg C33 A:619267 2.88 Mg C23 A:619267 4.20 Mg N17 A:619267 4.80 Mg O A:Hoh334 4.94 Mg O A:Hoh371 3.96 Mg O A:Hoh445 2.05 interactive model: