EC Number   |
Reference  |
|---|
    1.14.99.54 | structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides |
745861 |
| 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 1.2 A resolution, P21 space group with two protein molecules with non-crystallographic symmetry per asymmetric unit. Role for a conserved histidine in promoting oxygen activation |
739859 |
| 1.14.99.54 | to 1.3 A resolution |
741336 |
| 1.14.99.54 | to 1.75 A resolution. Stucture reveals a copper-bound active site common to LPMOs, a collection of aromatic and polar residues near the binding surface that may be responsible for regioselectivity, and substantial differences in loop structures near the binding face. Surface analysis reveals energy wells whose spacing seems adapted to the spacing of cellobiose units along a cellulose chain |
740707 |
| 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 |
