Copper in the structure of Crystal Structures Of The Copper-Containing Amine Oxidase From Arthrobacter Globiformis in The Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone (pdb 1avl)

The binding sites of Copper atom in the structure of Crystal Structures Of The Copper-Containing Amine Oxidase From Arthrobacter Globiformis in The Holo-and Apo-Forms: Implications For the Biogenesis of Topa Quinone (pdb code 1avl). This binding sites where shown with 5.0 Angstroms radius around Copper atom. The 1avl structure was solved by M.C.J.WILCE, J.M.GUSS, H.C.FREEMAN, with X-Ray Crystallography technique, brief refinement statistics is given in the table below: Resolution (A) 50.0-2.8 Space group C121 a (A) 158.200 b (A) 64.100 c (A) 92.900 alpha (°) 90.00 beta (°) 112.70 gamma (°) 90.00 Rfactor (%) 15 Rfree (%) 20.2 Copper Binding Sites: Copper binding site 1 out of 1 in 1avl Click to enlarge Click to enlarge Mono- and Stereo- picture of 5.0 Angstrom coordination sphere 1 of Copper in the PDB 1avl. Coordination sphere was calculated for all residues within 5.0 Angstroms distance from the central Copper atom, shown by VdW sphere Residues shown as a stick model or VDW spheres: A: Tpq382, A: His431, A: His433, A: His592, A: Met602, conact list: Atom Atom Distance (A) Cu O5 A:Tpq382 3.64 Cu C6 A:Tpq382 4.96 Cu C5 A:Tpq382 3.77 Cu C4 A:Tpq382 3.24 Cu C3 A:Tpq382 4.14 Cu O4 A:Tpq382 2.44 Cu NE2 A:His431 2.02 Cu ND1 A:His431 4.06 Cu CD2 A:His431 3.03 Cu CE1 A:His431 2.94 Cu CG A:His431 4.13 Cu NE2 A:His433 2.13 Cu ND1 A:His433 4.20 Cu CD2 A:His433 3.08 Cu CE1 A:His433 3.10 Cu CG A:His433 4.22 Cu NE2 A:His592 4.32 Cu CB A:His592 3.53 Cu ND1 A:His592 2.27 Cu ND1 A:His592 3.12 Cu CD2 A:His592 4.37 Cu CD2 A:His592 4.98 Cu CE1 A:His592 3.20 Cu CE1 A:His592 4.15 Cu CG A:His592 3.25 Cu CG A:His592 3.77 Cu CE A:Met602 4.63 Cu SD A:Met602 4.39 interactive model: