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EC Number
Metals/Ions
Commentary
Reference
Cu2+
strictly conserved copper-binding site which consists of two histidines (one at N-terminal position) and one tyrosine; strictly conserved copper-binding site which consists of two histidines (one at N-terminal position) and one tyrosine
Cu2+
The copper ion lies in the center of a flat surface that interacts with the substrate. The equatorial plane includes the protein's N-terminal Ndelta of His-1 and the Nepsilon of His-83
Cu2+
1 mol of copper per mol of proein; 1 mol of copper per mol of proein; 1 mol of copper per mol of protein
Cu2+
CuII oxidation state
Cu2+
Cu(II) saturation of enzyme prior to assay
Cu2+
type II copper center, which exhibits a hexacoordination
Cu2+
the active catalyst is Cu(II)-oxyl
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; the copper site of CelS2 is similar to that of chitin-active LPMO10s. Dissociation constant is 31 nM
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