eF-site ID 2jkp-AB PDB Code 2jkp Chain A, B click to enlarge Title Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine Classification HYDROLASE Compound ALPHA-GLUCOSIDASE (ALPHA-GLUCOSIDASE SUSB) Source Bacteroides thetaiotaomicron (P71094_BACTN) Sequence A:  QQKLTSPDNNLVMTFQVDSKGAPTYELTYKNKVVIKPSTL GLELKKEDSKTNLYDGFEVKDTQTATFDETWQPVWGEEKE IRNHYNELAVTLYQPMNDRSIVIRFRLFNDGLGFRYEFPQ QKSLNYFVIKEEHSQFGMNGDHIAFWIPGDYDTQEYDYTI SRLSEIRGLMKEAITPNSSQTPFSQTGVQTALMMKTDDGL YINLHEAALVDYSCMHLNLDDKNMVFESWLTPDAKGDKGY MQTPCNTPWRTIIVSDDARNILASRITLNLNEPCKIADAA SWVKPVKYIGVWWDMITGKGSWAYTDELTSVKLGETDYSK TKPNGKHSANTANVKRYIDFAAAHGFDAVLVEGWNEGWED WFGNSKDYVFDFVTPYPDFDVKEIHRYAARKGIKMMMHHE TSASVRNYERHMDKAYQFMADNGYNSVKSGYVGNIIPRGE HHYGQWMNNHYLYAVKKAADYKIMVNAHEATRPTGICRTY PNLIGNESARGTEYESFGGNKVYHTTILPFTRLVGGPMDY TPGIFETHCNKMNPANNSQVRSTIARQLALYVTMYSPLQM AADIPENYERFMDAFQFIKDVALDWDETNYLEAEPGEYIT IARKAKDTDDWYVGCTAGENGHTSKLVFDFLTPGKQYIAT VYADAKDADWKENPQAYTIKKGILTNKSKLNLHAANGGGY AISIKEV B:  QQKLTSPDNNLVMTFQVDSKGAPTYELTYKNKVVIKPSTL GLELKKEDSKTNLYDGFEVKDTQTATFDETWQPVWGEEKE IRNHYNELAVTLYQPMNDRSIVIRFRLFNDGLGFRYEFPQ QKSLNYFVIKEEHSQFGMNGDHIAFWIPGDYDTQEYDYTI SRLSEIRGLMKEAITPNSSQTPFSQTGVQTALMMKTDDGL YINLHEAALVDYSCMHLNLDDKNMVFESWLTPDAKGDKGY MQTPCNTPWRTIIVSDDARNILASRITLNLNEPCKIADAA SWVKPVKYIGVWWDMITGKGSWAYTDELTSVKLGETDYSK TKPNGKHSANTANVKRYIDFAAAHGFDAVLVEGWNEGWED WFGNSKDYVFDFVTPYPDFDVKEIHRYAARKGIKMMMHHE TSASVRNYERHMDKAYQFMADNGYNSVKSGYVGNIIPRGE HHYGQWMNNHYLYAVKKAADYKIMVNAHEATRPTGICRTY PNLIGNESARGTEYESFGGNKVYHTTILPFTRLVGGPMDY TPGIFETHCNKMNPANNSQVRSTIARQLALYVTMYSPLQM AADIPENYERFMDAFQFIKDVALDWDETNYLEAEPGEYIT IARKAKDTDDWYVGCTAGENGHTSKLVFDFLTPGKQYIAT VYADAKDADWKENPQAYTIKKGILTNKSKLNLHAANGGGY AISIKEV Description Functional site 1) chain A residue 331 type sequence W description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 2) chain A residue 335 type sequence I description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 3) chain A residue 341 type sequence W description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 4) chain A residue 391 type sequence E description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 5) chain A residue 397 type sequence W description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 6) chain A residue 400 type sequence W description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 7) chain A residue 437 type sequence H description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 8) chain A residue 439 type sequence E description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 9) chain A residue 467 type sequence K description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 10) chain A residue 471 type sequence V description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 11) chain A residue 507 type sequence H description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 12) chain A residue 508 type sequence E description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 13) chain A residue 526 type sequence E description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 14) chain A residue 532 type sequence E description BINDING SITE FOR RESIDUE CTS A1727 source : AC1 15) chain B residue 331 type sequence W description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 16) chain B residue 335 type sequence I description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 17) chain B residue 341 type sequence W description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 18) chain B residue 391 type sequence E description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 19) chain B residue 397 type sequence W description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 20) chain B residue 400 type sequence W description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 21) chain B residue 437 type sequence H description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 22) chain B residue 439 type sequence E description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 23) chain B residue 467 type sequence K description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 24) chain B residue 471 type sequence V description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 25) chain B residue 507 type sequence H description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 26) chain B residue 508 type sequence E description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 27) chain B residue 526 type sequence E description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 28) chain B residue 532 type sequence E description BINDING SITE FOR RESIDUE CTS B1727 source : AC2 29) chain B residue 194 type sequence E description BINDING SITE FOR RESIDUE CA B1728 source : AC3 30) chain B residue 508 type sequence E description BINDING SITE FOR RESIDUE CA B1728 source : AC3 31) chain B residue 526 type sequence E description BINDING SITE FOR RESIDUE CA B1728 source : AC3 32) chain B residue 532 type sequence E description BINDING SITE FOR RESIDUE CA B1728 source : AC3 33) chain A residue 194 type sequence E description BINDING SITE FOR RESIDUE CA A1728 source : AC4 34) chain A residue 508 type sequence E description BINDING SITE FOR RESIDUE CA A1728 source : AC4 35) chain A residue 526 type sequence E description BINDING SITE FOR RESIDUE CA A1728 source : AC4 36) chain A residue 532 type sequence E description BINDING SITE FOR RESIDUE CA A1728 source : AC4 37) chain A residue 112 type sequence P description BINDING SITE FOR RESIDUE EDO A1729 source : AC5 38) chain A residue 113 type sequence V description BINDING SITE FOR RESIDUE EDO A1729 source : AC5 39) chain A residue 114 type sequence W description BINDING SITE FOR RESIDUE EDO A1729 source : AC5 40) chain A residue 516 type sequence C description BINDING SITE FOR RESIDUE EDO A1729 source : AC5 41) chain A residue 520 type sequence P description BINDING SITE FOR RESIDUE EDO A1729 source : AC5 42) chain A residue 333 type sequence D description BINDING SITE FOR RESIDUE EDO A1730 source : AC6 43) chain A residue 338 type sequence K description BINDING SITE FOR RESIDUE EDO A1730 source : AC6 44) chain A residue 372 type sequence N description BINDING SITE FOR RESIDUE EDO A1730 source : AC6 45) chain A residue 376 type sequence Y description BINDING SITE FOR RESIDUE EDO A1730 source : AC6 46) chain A residue 603 type sequence I description BINDING SITE FOR RESIDUE EDO A1730 source : AC6 47) chain B residue 112 type sequence P description BINDING SITE FOR RESIDUE EDO B1729 source : AC7 48) chain B residue 113 type sequence V description BINDING SITE FOR RESIDUE EDO B1729 source : AC7 49) chain B residue 114 type sequence W description BINDING SITE FOR RESIDUE EDO B1729 source : AC7 50) chain B residue 516 type sequence C description BINDING SITE FOR RESIDUE EDO B1729 source : AC7 51) chain B residue 520 type sequence P description BINDING SITE FOR RESIDUE EDO B1729 source : AC7 52) chain B residue 333 type sequence D description BINDING SITE FOR RESIDUE EDO B1730 source : AC8 53) chain B residue 338 type sequence K description BINDING SITE FOR RESIDUE EDO B1730 source : AC8 54) chain B residue 372 type sequence N description BINDING SITE FOR RESIDUE EDO B1730 source : AC8 55) chain B residue 376 type sequence Y description BINDING SITE FOR RESIDUE EDO B1730 source : AC8 56) chain A residue 532 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000305|PubMed:18981178 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 532 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000305|PubMed:18981178 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 194 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 508 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 526 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 532 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 194 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 63) chain B residue 508 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 64) chain B residue 526 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 532 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18981178 source Swiss-Prot : SWS_FT_FI2 66) chain A residue 215 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 67) chain A residue 437 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 68) chain A residue 507 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 69) chain B residue 215 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 70) chain B residue 437 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 71) chain B residue 507 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 72) chain A residue 194 type SITE sequence E description Substrate source Swiss-Prot : SWS_FT_FI4 73) chain A residue 331 type SITE sequence W description Substrate source Swiss-Prot : SWS_FT_FI4 74) chain A residue 467 type SITE sequence K description Substrate source Swiss-Prot : SWS_FT_FI4 75) chain B residue 194 type SITE sequence E description Substrate source Swiss-Prot : SWS_FT_FI4 76) chain B residue 331 type SITE sequence W description Substrate source Swiss-Prot : SWS_FT_FI4 77) chain B residue 467 type SITE sequence K description Substrate source Swiss-Prot : SWS_FT_FI4

Display surface Download Links