eF-site ID 1cgt-A PDB Code 1cgt Chain A click to enlarge Title STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE REFINED AT 2.0 ANGSTROMS RESOLUTION Classification GLYCOSYLTRANSFERASE Compound CYCLODEXTRIN GLYCOSYL-TRANSFERASE Source null (CDGT1_BACCI) Sequence A:  DPDTAVTNKQSFSTDVIYQVFTDRFLDGNPSNNPTGAAYD ATCSNLKLYCGGDWQGLINKINDNYFSDLGVTALWISQPV ENIFATINYSGVTNTAYHGYWARDFKKTNPYFGTMADFQN LITTAHAKGIKIVIDFAPNHTSPAMETDTSFAENGRLYDN GTLVGGYTNDTNGYFHHNGGSDFSSLENGIYKNLYDLADF NHNNATIDKYFKDAIKLWLDMGVDGIRVDAVKHMPLGWQK SWMSSIYAHKPVFTFGEWFLGSAASDADNTDFANKSGMSL LDFRFNSAVRNVFRDNTSNMYALDSMINSTATDYNQVNDQ VTFIDNHDMDRFKTSAVNNRRLEQALAFTLTSRGVPAIYY GTEQYLTGNGDPDNRAKMPSFSKSTTAFNVISKLAPLRKS NPAIAYGSTQQRWINNDVYVYERKFGKSVAVVAVNRNLST SASITGLSTSLPTGSYTDVLGGVLNGNNITSTNGSINNFT LAAGATAVWQYTTAETTPTIGHVGPVMGKPGNVVTIDGRG FGSTKGTVYFGTTAVTGAAITSWEDTQIKVTIPSVAAGNY AVKVAASGVNSNAYNNFTILTGDQVTVRFVVNNASTTLGQ NLYLTGNVAELGNWSTGSTAIGPAFNQVIHQYPTWYYDVS VPAGKQLEFKFFKKNGSTITWESGSNHTFTTPASGTATVT VNWQ Description (1)  CYCLODEXTRIN GLYCOSYLTRANSFERASE (E.C.2.4.1.19) Functional site 1) chain A residue 139 type sequence N description BINDING SITE FOR RESIDUE CA A 685 source : AC1 2) chain A residue 190 type sequence I description BINDING SITE FOR RESIDUE CA A 685 source : AC1 3) chain A residue 199 type sequence D description BINDING SITE FOR RESIDUE CA A 685 source : AC1 4) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE CA A 685 source : AC1 5) chain A residue 27 type sequence D description BINDING SITE FOR RESIDUE CA A 686 source : AC2 6) chain A residue 29 type sequence N description BINDING SITE FOR RESIDUE CA A 686 source : AC2 7) chain A residue 32 type sequence N description BINDING SITE FOR RESIDUE CA A 686 source : AC2 8) chain A residue 33 type sequence N description BINDING SITE FOR RESIDUE CA A 686 source : AC2 9) chain A residue 51 type sequence G description BINDING SITE FOR RESIDUE CA A 686 source : AC2 10) chain A residue 53 type sequence D description BINDING SITE FOR RESIDUE CA A 686 source : AC2 11) chain A residue 229 type ACT_SITE sequence D description Nucleophile => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 257 type ACT_SITE sequence E description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 32 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 14) chain A residue 33 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 15) chain A residue 190 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 16) chain A residue 196 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 17) chain A residue 199 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 18) chain A residue 232 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 19) chain A residue 233 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 327 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 371 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 375 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 51 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 24) chain A residue 53 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 25) chain A residue 100 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 139 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 140 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 27 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 29) chain A residue 29 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 30) chain A residue 193 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 227 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 328 type SITE sequence D description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI5

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