EC Number   |
|---|
   1.14.99.53 | homology modeling. Residues His1 and His61 directly coordinate the basic copper cofactor in T-shaped geometry. The axial, noncoordinating active site residue is Tyr142 |
| 1.14.99.53 | homology modeling, CbpD is a monomeric tri-modular enzyme with flexible linkers |
| 1.14.99.53 | homology modeling reveals the typical central beta-sandwich fold of LPMOs, as well as flexible loops and two stabilizing disulfide bonds. The active site contains the histidine brace, consisting of His1 and His96 coordinating the copper cofactor, and the axial, non-coordinating residue Phe187 |
| 1.14.99.53 | homology modeling and molecular docking, a binding site for the chitin heptamer exists near the histidine brace active site |
| 1.14.99.53 | crystallization at pH 3.5. Structure shows shows significant disorder of the active site in the absence of substrate ligand |
| 1.14.99.53 | crystal structure in the Cu(II)-bound form and photoreduction of the crystalline protein in the x-ray beam, leading to conversion from the initial Cu(II)-oxidized form with two coordinated water molecules, which adopts a trigonal bipyramidal geometry, to a reduced Cu(I) form in a T-shaped geometry with no coordinated water molecules |
| 1.14.99.53 | comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues |
| 1.14.99.53 | calculation of solution structure. Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ ions show binding to an interaction site located between His28 and His114 |
| 1.14.99.53 | analysis of the copper active site |
| 1.14.99.53 | 1.55 A resolution structure of N-terminal LPMO10A module reveals deletions of interacting loops that protrude from the core beta-sandwich scaffold in larger LPMO10s |
