1.14.99.53	Ca2+	presence promotes saccharification efficiency of chitin by 36.7%	766324	
1.14.99.53	copper	-	744375, 767577	
1.14.99.53	copper	Cu2+ does not dissociate from the protein molecule during unfolding	766321	
1.14.99.53	copper	His1 and His96 coordinate the copper cofactor	766292	
1.14.99.53	copper	the active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry	745380	
1.14.99.53	copper	tight binding activity toward Cu2+ , Kd value 0.0048 mM. Residues His1 and His61 directly coordinate the basic copper cofactor in T-shaped geometry	766407	
1.14.99.53	Cu2+	-	745380	
1.14.99.53	Cu2+	crystal structures show a putative dioxygen species equatorially bound to the active site copper	740090	
1.14.99.53	Cu2+	Cu(II) binds with KD value 43 nM at pH 5. The coordination geometry around the copper is distorted from axial symmetry	740345	
1.14.99.53	Cu2+	dependent on	736250, 736633	
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	
1.14.99.53	additional information	enzyme is highly tolerant and stable in presence of up to 1 M metal ions	766324	
1.14.99.53	additional information	no binding activity toward Zn2+	766407	
1.14.99.53	additional information	residues His28 and His114 in the catalytic center bind a variety of divalent metal ions such as Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ with a clear preference for Cu2+	741326	
1.14.99.53	Na+	presence promotes saccharification efficiency of chitin by 22.6%	766324	
1.14.99.53	Zn2+	may substitue for Cu2+. KD value 0.0081 mM at pH 5	740345