Table 2.

Functionally important amino and amino acids in the S_1-, S₁′- and S₂′-subpockets of TLN, PLN, ALN, MMP-9, and MMP-14 contributing to the binding of catechol or bisphosphonate containing compounds tested in the present study.

	TLN	PLN	ALN	MMP-9	MMP-14
S1-subpocket	W115, Y157	W115, Y155	W117, Q152, N167	H190, P193	F204
S1′-subpocket	L133, V139, H142, I188	L132, V137, H140, I190	V137, H144, I186, V189	L397, V398, H401, L418, Y420, P421, Y423, R424, T426	L199, E219, W221, N231, H239
S2′-subpocket	N111, F130, Y193, L202	E111, F129, L197	N114, F132, L199	G186, L187, Y218	L235, V236, Y261, Q262
Catalytic Glu	E143	E141	E145	E402	E240
Known inhibitor binding residues	N112, A113, F114, R203, H231	E111, N112, A113, R198, H223	N112, Y114, R200, H228	A189, H190, A191	A200, H201
Zn2+ ligated	H142, H146, E166	H140, H144, E164	H144, H148, E168	H401, H405, H411	H239, H243, H248

The subpocket amino acids of MMP-9 in the table are based on the X-ray structure of the inactive MMP-9 mutant E402A lacking the pro, FnII, hinge and HPX domains bound to a chromogenic substrate (PDB id: 4JIJ)⁷¹, while the numbering is as in the PDB id: 1l6j, which includes the three FnII-like repeats in the catalytic site⁷². The subpocket amino acids of TLN are based on Krimmer et al.⁷³. Subpocket amino acids of the other enzymes are based on structural superimposition with TLN (PLN and ALN) and MMP-9 (MMP-14).