eF-site ID 1eo7-A PDB Code 1eo7 Chain A click to enlarge Title BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE IN COMPLEX WITH MALTOHEXAOSE Classification TRANSFERASE Compound PROTEIN (CYCLODEXTRIN GLYCOSYLTRANSFERASE) Source (CDGU_BACCI) Sequence A:  APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFD GTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPV ENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQN LIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDN GTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADL NHNNSTVDVYLKDAIKMWLDLGIDGIRMAAVKHMPFGWQK SFMAAVNNYKPVFTFGAWFLGVNEVSPENHKFANESGMSL LDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQ VTFIDNHDMERFHASNANRRKLEQALAFTLTSRGVPAIYY GTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKS NPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNA PASISGLVTSLPQGSYNDVLGGLLNGNTLSVGSGGAASNF TLAAGGTAVWQYTAATATPTIGHVGPMMAKPGVTITIDGR GFGSSKGTVYFGTTAVSGADITSWEDTQIKVKIPAVAGGN YNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTAL GQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDV SVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATI NVNWQP Description Functional site 1) chain A residue 227 type catalytic sequence R description 45 source MCSA : MCSA1 2) chain A residue 229 type catalytic sequence A description 45 source MCSA : MCSA1 3) chain A residue 257 type catalytic sequence A description 45 source MCSA : MCSA1 4) chain A residue 327 type catalytic sequence H description 45 source MCSA : MCSA1 5) chain A residue 328 type catalytic sequence D description 45 source MCSA : MCSA1 6) chain A residue 27 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 7) chain A residue 145 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 8) chain A residue 190 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 9) chain A residue 193 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 10) chain A residue 199 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 11) chain A residue 227 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 12) chain A residue 232 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 13) chain A residue 233 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 14) chain A residue 315 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 15) chain A residue 327 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 16) chain A residue 371 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 17) chain A residue 29 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 18) chain A residue 375 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 19) chain A residue 577 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 32 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 33 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 51 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 53 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 24) chain A residue 100 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 25) chain A residue 139 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 140 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 328 type SITE sequence D description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 229 type ACT_SITE sequence A description Nucleophile source Swiss-Prot : SWS_FT_FI1 29) chain A residue 257 type ACT_SITE sequence A description Proton donor source Swiss-Prot : SWS_FT_FI2

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