EC Number |
Reference |
---|
1.14.99.54 | hybrid quantum mechanics and molecular mechanics investigation of the first steps of the LPMO mechanism, which is reduction of CuII to CuI and the formation of a CuII-superoxide complex. In the complex, the superoxide can bind either in an equatorial or an axial position. The equatorial isomer of the superoxide complex is over 60 kJ/mol more stable than the axial isomer because it is stabilized by interactions with a second-coordination-sphere glutamine residue |
743929 |
1.14.99.54 | C-terminally truncated variant containing 21 residues of the predicted linker domain, to 0.95 A resolution. The linker forms an integral part of the catalytic domain structure, covering a hydrophobic patch on the catalytic AA9 module. The oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand |
745374 |
1.14.99.54 | structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry |
745380 |
1.14.99.54 | to 3.0 A resolution. The active site of AA14B is constituted by His1, His99 and Tyr176, forming the canonical histidine brace that is exposed at the surface |
745847 |
1.14.99.54 | structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides |
745861 |
1.14.99.54 | single-molecule study by atomic force microscopy |
745866 |