EC Number |
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1.14.99.B10 | 1H, 13C, and 15N chemical shift assignments of the apo-form of the catalytic doman |
1.14.99.B10 | crystals grown in presence of Zn2+ and of Cu2+. Structure of the catalytic domain reveals an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. Binding affinities are in the low micromolar range for polymeric substrates due in part to the presence of a carbohydrate-binding module |
1.14.99.B10 | docking studies with cellulose hexamer. The surface patch surrounding the copper site appears to be a preferred interaction surface. Residue Tyr204 appears not to be involved in binding of this substrate |
1.14.99.B10 | structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides |