Investigation into Structural Changes of the Copper Binding Site in Lysyl Oxidase upon Substrate and Inhibitor Docking

Table 1

The list of various docked substrates and inhibitors, and their effect on the conformational rearrangements GLN104 and TYR35. Distances were measured between the hydroxyl oxygen of TYR35 and the oxygen bound to the 𝛿-carbon of GLN104.

Name	Abbreviation	GLN104-TYR35 distance (Å)
Lysyl oxidase (control)	LOX	9.00
𝛽-Aminopropionitrile	BAPN	8.90
Bromoethylamine	BEA	9.10
Chloroethylamine	CEA	5.60
Ethylenediamine	EDA	5.70
3-Aminodihydrofuran-2-one	ADF	5.70
3-Aminodihydrothiophen-2-one	ADT	5.90
Nitroethylamine	NEA	5.50
para-Bromobenzylamine	pBBA	5.70
para-Chlorobenzylamine	pCBA	5.50
para-Fluorobenzylamine	pFBA	5.70
para-Methylbenzylamine	pMBA	5.50
trans-2-Phenylcyclopropylamine	tPCPA	5.40