eF-site ID 1tr1-ABCD PDB Code 1tr1 Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURE OF E96K MUTATED BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA, AN ENZYME WITH INCREASED THERMORESISTANCE Classification FAMILY 1 BETA-GLUCOSIDASE Compound BETA-GLUCOSIDASE A Source Paenibacillus polymyxa (Bacillus polymyxa) (BGLA_PAEPO) Sequence A:  TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHT PGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVS WPRIFPNGDGEVNQKGLDYYHRVVDLLNDNGIEPFCTLYH WDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHW LTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACAR TISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDM DIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLPV TDIGWPVESRGLYEVLHYLQKYGNIDIYITENGACINDEV VNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLL DNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSN NWLETRR B:  TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHT PGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVS WPRIFPNGDGEVNQKGLDYYHRVVDLLNDNGIEPFCTLYH WDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHW LTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACAR TISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDM DIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLPV TDIGWPVESRGLYEVLHYLQKYGNIDIYITENGACINDEV VNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLL DNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSN NWLETRR C:  TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHT PGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVS WPRIFPNGDGEVNQKGLDYYHRVVDLLNDNGIEPFCTLYH WDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHW LTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACAR TISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDM DIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLPV TDIGWPVESRGLYEVLHYLQKYGNIDIYITENGACINDEV VNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLL DNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSN NWLETRR D:  TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHT PGKVFNGDNGNVACDSYHRYEEDIRLMKELGIRTYRFSVS WPRIFPNGDGEVNQKGLDYYHRVVDLLNDNGIEPFCTLYH WDLPQALQDAGGWGNRRTIQAFVQFAETMFREFHGKIQHW LTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACAR TISLHSDWFLQPIYQGSYPQFLVDWFAEQGATVPIQDGDM DIIGEPIDMIGINYYSMSVNRFNPEAGFLQSEEINMGLPV TDIGWPVESRGLYEVLHYLQKYGNIDIYITENGACINDEV VNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLL DNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSN NWLETRR Description Functional site 1) chain A residue 20 type sequence Q description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 2) chain A residue 296 type sequence Y description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 3) chain A residue 326 type sequence W description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 4) chain A residue 352 type sequence E description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 5) chain A residue 398 type sequence W description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 6) chain A residue 405 type sequence E description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 7) chain A residue 406 type sequence W description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 8) chain A residue 414 type sequence F description BINDING SITE FOR RESIDUE GOL A 2000 source : AC1 9) chain B residue 20 type sequence Q description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 10) chain B residue 296 type sequence Y description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 11) chain B residue 326 type sequence W description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 12) chain B residue 352 type sequence E description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 13) chain B residue 398 type sequence W description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 14) chain B residue 405 type sequence E description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 15) chain B residue 406 type sequence W description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 16) chain B residue 414 type sequence F description BINDING SITE FOR RESIDUE GOL B 2000 source : AC2 17) chain C residue 20 type sequence Q description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 18) chain C residue 296 type sequence Y description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 19) chain C residue 326 type sequence W description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 20) chain C residue 352 type sequence E description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 21) chain C residue 398 type sequence W description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 22) chain C residue 405 type sequence E description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 23) chain C residue 406 type sequence W description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 24) chain C residue 414 type sequence F description BINDING SITE FOR RESIDUE GOL C 2000 source : AC3 25) chain D residue 20 type sequence Q description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 26) chain D residue 296 type sequence Y description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 27) chain D residue 326 type sequence W description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 28) chain D residue 352 type sequence E description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 29) chain D residue 398 type sequence W description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 30) chain D residue 405 type sequence E description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 31) chain D residue 406 type sequence W description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 32) chain D residue 414 type sequence F description BINDING SITE FOR RESIDUE GOL D 2000 source : AC4 33) chain A residue 166 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 166 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 35) chain C residue 166 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 166 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 352 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 352 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 352 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 40) chain D residue 352 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 348-356 type prosite sequence IYITENGAC description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGAC source prosite : PS00572 42) chain A residue 10-24 type prosite sequence FMWGTATAAYQIEGA description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmWGtAtAAYQiEgA source prosite : PS00653

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