eF-site ID 1uwu-AB PDB Code 1uwu Chain A, B click to enlarge Title Structure of beta-glycosidase from Sulfolobus solfataricus in complex with D-glucohydroximo-1,5-lactam Classification HYDROLASE Compound BETA-GALACTOSIDASE Source null (BGAM_SULSO) Sequence A:  MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDP ENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARL NVEWSRIFPNPLPRPFDESKQDVTEVEINENELKRLDEYA NKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDPIR VRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYS TMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQA HARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEMAE NDNRWWFFDAIIRGEITKIVRDDLKGRLDWIGVNYYTRTV VKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFGWEFFPE GLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVSHV YQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKV DYNTKRLYWRPSALVYREIATNGAITDEIEHLNSVPPVKP LRH B:  MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDP ENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARL NVEWSRIFPNPLPRPFDESKQDVTEVEINENELKRLDEYA NKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDPIR VRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYS TMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQA HARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEMAE NDNRWWFFDAIIRGEITRGNEKIVRDDLKGRLDWIGVNYY TRTVVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFGWE FFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYL VSHVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFG LLKVDYNTKRLYWRPSALVYREIATNGAITDEIEHLNSVP PVKPLRH Description Functional site 1) chain A residue 342 type sequence H description BINDING SITE FOR RESIDUE ACT A 1491 source : AC1 2) chain A residue 361 type sequence W description BINDING SITE FOR RESIDUE ACT A 1491 source : AC1 3) chain A residue 410 type sequence H description BINDING SITE FOR RESIDUE ACT A 1492 source : AC2 4) chain A residue 411 type sequence R description BINDING SITE FOR RESIDUE ACT A 1492 source : AC2 5) chain B residue 322 type sequence Y description BINDING SITE FOR RESIDUE ACT B 1491 source : AC3 6) chain B residue 342 type sequence H description BINDING SITE FOR RESIDUE ACT B 1491 source : AC3 7) chain A residue 18 type sequence Q description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 8) chain A residue 150 type sequence H description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 9) chain A residue 205 type sequence N description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 10) chain A residue 206 type sequence E description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 11) chain A residue 322 type sequence Y description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 12) chain A residue 361 type sequence W description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 13) chain A residue 387 type sequence E description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 14) chain A residue 425 type sequence W description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 15) chain A residue 432 type sequence E description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 16) chain A residue 433 type sequence W description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 17) chain A residue 441 type sequence F description BINDING SITE FOR RESIDUE GOX A 1490 source : AC4 18) chain B residue 18 type sequence Q description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 19) chain B residue 150 type sequence H description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 20) chain B residue 151 type sequence W description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 21) chain B residue 205 type sequence N description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 22) chain B residue 206 type sequence E description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 23) chain B residue 322 type sequence Y description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 24) chain B residue 361 type sequence W description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 25) chain B residue 387 type sequence E description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 26) chain B residue 425 type sequence W description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 27) chain B residue 432 type sequence E description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 28) chain B residue 433 type sequence W description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 29) chain B residue 441 type sequence F description BINDING SITE FOR RESIDUE GOX B 1490 source : AC5 30) chain B residue 206 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 206 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 387 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 387 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 273 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 311 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 116 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 273 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 311 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 39) chain A residue 116 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 332 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 41) chain B residue 135 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 42) chain B residue 332 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 135 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 383-391 type prosite sequence MYVTENGIA description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA source prosite : PS00572 45) chain A residue 8-22 type prosite sequence FRFGWSQAGFQSEMG description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FrFGwSqAGFQsEmG source prosite : PS00653 46) chain B residue 76 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 47) chain B residue 102 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 48) chain B residue 124 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 49) chain B residue 138 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 50) chain A residue 76 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 51) chain A residue 102 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 52) chain A residue 124 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 53) chain A residue 138 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3

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