EC Number   |
Metals/Ions   |
Reference   |
|---|
 1.14.99.53 | Cu2+ |
Kd value 55 nM, from isothermal titration calorimetry, and for Cu1+, Kd value 1 nM from the experimentally determined redox potential |
741326 |
 1.14.99.53 | Cu2+ |
KD value 790 pM at pH 5 |
741038 |
 1.14.99.53 | Cu2+ |
saturation of enzyme with cu2+ prior to assay |
740448 |
 1.14.99.53 | Cu2+ |
structural changes observed upon irradiation of CBM33A reflect photoreduction of Cu(II) to Cu(I). Charges found in the formal Cu(II) and Cu(I) oxidation states are 1.48 and 0.92, respectively |
736451 |
 1.14.99.53 | Cu2+ |
structure of the copper-binding site |
736451 |
 1.14.99.53 | Cu2+ |
the active site contains a copper ion coordinated by residues His-37 and His-136 in a T-shaped histidine brace |
740758 |
 1.14.99.53 | Cu2+ |
the active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry |
745380 |
 1.14.99.53 | Cu2+ |
the copper site is highly similar to that of the C1/C4 cellulose-oxidizing LPMO9A from Thermoascus aurantiacus and exhibits an octahedral coordination geometry with Jahn-Teller distortion. Dissociation constant is 12 nM |
741336 |
 1.14.99.53 | K+ |
presence promotes saccharification efficiency of chitin by 45.9% |
766324 |
 1.14.99.53 | Mg2+ |
presence promotes saccharification efficiency of chitin by 53.9% |
766324 |