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. 2014 May 7;9(5):e96627. doi: 10.1371/journal.pone.0096627

Table 4. Residues from the active sites of β-glucosidases in direct contact with sector A positions.

Sector A position Active site residues
SfβGly 1UG6 1E4I 1E56 1V03 1E6S 2ZOX 3AHY
54 K201abr, M453abr H178abr, A394abr H179, A407 F205abr, F466abr L203abr, S462abr D201, N466 F179abr, N426 F179, A426
98 R97p R75 R77 R96 R97 R95 R75 R73
143 H142bg, E187*, E190abr, K201abr H119bg, E164*, C167, H178abr H121bg, E166*, C168, H179 H142bg, D191*, T194, F205abr H143bg, D189*, T192, L203abr H141bg, Q187, S190abr, D201 H120bg, Q165*, F179abr H119bg, E165*, C168, F179
188 E187*, E190abr E164*, C167 E166*, C168 D191*, T194 D189*, T192 Q187, S190abr Q165*, V168abr E165*, C168
195 E194abr C167, L171abr, H178 C168, L172, H179 T194, F198abr, F205abr T192, V196abr, L203abr S190abr, R194abr, D201 M172abr, F179abr C168, P172, F179
196 E194abr L171abr L172 F198abr V196abr R194abr M172abr P172
203 E194abr, K201abr H178abr H179 F205abr L203abr D201 F179abr F179
398 R97p, E399* R75, E338* R77, E352* R96, E406* R97, E404* R95, E409* E373* R73, E367*
451 Q39bg, W444bg, M453abr Q18bg, W385bg, A394abr Q20bg, W398bg, A407 Q38bg, W457bg, F466abr Q39bg, W453, S462abr Q39bg, W457bg, N466 Q17, W417bg, N426 Q16bg, W417bg, N426
452 Q39bg, H142bg, K201abr, M453abr Q18bg, H119bg, H178abr, A394abr Q20bg, H121bg, H180, A407 Q38bg, H142bg, F205abr, F466abr Q39bg, H143bg, L203abr, S462abr Q39bg, H141bg, N466 Q17, H120bg, F179abr, N426 Q16bg, H119bg, F179, N426
460 Y331p, W444bg Y284, W385bg Y296, W398bg Y333, W457bg Y331, W453bg W457bg Y309, W417bg Y298, W417bg

The numbering of the sector A positions was based on the Sfβgly sequence. * identifies catalytic glutamic acids; p – indicates residues involved in the modulation of the pK a of the catalytic glutamic acids; bg – shows residues involved in the binding of the substrate glycone; abr – indicates residues that form the aglycone binding region. Data regarding the role of individual residues in substrate binding and catalysis were retrieved from the literature [5], [27], [28], [29], [9], [30]. β-Glucosidase from Spodoptera frugiperda Sfβgly; β-glucosidase from Thermus thermophilus (1UG6); β-glucosidase A from Paenibacillus polymyxa (1E4I); β-glucosidase Zmglu from Zea mays (1E56); β-glucosidase SbDhr from Sorghum bicolor (1V03); myrosinase from Sinapis alba (1E6S); Human cytosolic β-glucosidase (2ZOX);β-glucosidase from Trichoderma reesei (3AHY).