Copper in the structure of Glactose Oxidase C383S Mutant Identified By Directed Evolution (pdb 1t2x)

The binding sites of Copper atom in the structure of Glactose Oxidase C383S Mutant Identified By Directed Evolution (pdb code 1t2x). This binding sites where shown with 5.0 Angstroms radius around Copper atom. The 1t2x structure was solved by D.WILKINSON, N.AKUMANYI, R.HURTADO-GUERRERO, H.DAWKES, P.F.KNOWLES, S.E.V.PHILLIPS, M.J.MCPHERSON, with X-Ray Crystallography technique, brief refinement statistics is given in the table below: Resolution (A) 62.0-2.3 Space group C121 a (A) 97.376 b (A) 88.995 c (A) 85.800 alpha (°) 90.00 beta (°) 117.49 gamma (°) 90.00 Rfactor (%) 21.8 Rfree (%) 22.8 Copper Binding Sites: Copper binding site 1 out of 1 in 1t2x Click to enlarge Click to enlarge Mono- and Stereo- picture of 5.0 Angstrom coordination sphere 1 of Copper in the PDB 1t2x. 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: Phe227, A: Cys228, A: Tyr272, A: Tyr405, A: Tyr495, A: His496, A: His581, A: Act643, A: Hoh956, conact list: Atom Atom Distance (A) Cu CE2 A:Phe227 4.20 Cu CZ A:Phe227 3.42 Cu CE1 A:Phe227 4.10 Cu SG A:Cys228 3.37 Cu CE2 A:Tyr272 3.90 Cu CD1 A:Tyr272 4.70 Cu CZ A:Tyr272 2.89 Cu CE1 A:Tyr272 3.42 Cu OH A:Tyr272 2.00 Cu OH A:Tyr405 4.83 Cu CE2 A:Tyr495 3.55 Cu CD2 A:Tyr495 4.67 Cu CZ A:Tyr495 3.29 Cu CE1 A:Tyr495 4.25 Cu OH A:Tyr495 2.73 Cu NE2 A:His496 1.98 Cu ND1 A:His496 4.09 Cu CD2 A:His496 2.91 Cu CE1 A:His496 3.02 Cu CG A:His496 4.07 Cu NE2 A:His581 2.13 Cu ND1 A:His581 4.23 Cu CD2 A:His581 2.93 Cu CE1 A:His581 3.23 Cu CG A:His581 4.13 Cu O A:Act643 4.75 Cu C A:Act643 4.84 Cu OXT A:Act643 4.15 Cu O A:Hoh956 3.30 interactive model: