eF-site ID 1cxl-A PDB Code 1cxl Chain A click to enlarge Title COMPLEX BETWEEN A COVALENT INTERMEDIATE AND BACILLUS CIRCULANS STRAIN 251 CGTASE E257Q Classification GLYCOSYLTRANSFERASE Compound PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE) Source (CDGU_BACCI) Sequence A:  APDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFD GTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPV ENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQN LIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDN GTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADL NHNNSTVDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQK SFMAAVNNYKPVFTFGQWFLGVNEVSPENHKFANESGMSL LDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQ VTFIDNHDMERFHASNANRRKLEQALAFTLTSRGVPAIYY GTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKS NPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNA PASISGLVTSLPQGSYNDVLGGLLNGNTLSVGSGGAASNF TLAAGGTAVWQYTAATATPTIGHVGPMMAKPGVTITIDGR GFGSSKGTVYFGTTAVSGADITSWEDTQIKVKIPAVAGGN YNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTAL GQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDV SVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATI NVNWQP Description Functional site 1) chain A residue 229 type sequence D description CATALYTIC SITE CONTAINING MUTANT E257Q source : CAT 2) chain A residue 257 type sequence Q description CATALYTIC SITE CONTAINING MUTANT E257Q source : CAT 3) chain A residue 328 type sequence D description CATALYTIC SITE CONTAINING MUTANT E257Q source : CAT 4) chain A residue 27 type sequence D description FIRST CALCIUM BINDING SITE. source : CA1 5) chain A residue 29 type sequence N description FIRST CALCIUM BINDING SITE. source : CA1 6) chain A residue 32 type sequence N description FIRST CALCIUM BINDING SITE. source : CA1 7) chain A residue 33 type sequence N description FIRST CALCIUM BINDING SITE. source : CA1 8) chain A residue 51 type sequence G description FIRST CALCIUM BINDING SITE. source : CA1 9) chain A residue 53 type sequence D description FIRST CALCIUM BINDING SITE. source : CA1 10) chain A residue 139 type sequence N description SECOND CALCIUM BINDING SITE. source : CA2 11) chain A residue 190 type sequence I description SECOND CALCIUM BINDING SITE. source : CA2 12) chain A residue 199 type sequence D description SECOND CALCIUM BINDING SITE. source : CA2 13) chain A residue 233 type sequence H description SECOND CALCIUM BINDING SITE. source : CA2 14) chain A residue 382 type sequence S description FIRST MALTOSE BINDING SITE. source : 16 15) chain A residue 616 type sequence W description FIRST MALTOSE BINDING SITE. source : 16 16) chain A residue 651 type sequence K description FIRST MALTOSE BINDING SITE. source : 16 17) chain A residue 662 type sequence W description FIRST MALTOSE BINDING SITE. source : 16 18) chain A residue 663 type sequence E description FIRST MALTOSE BINDING SITE. source : 16 19) chain A residue 667 type sequence N description FIRST MALTOSE BINDING SITE. source : 16 20) chain A residue 598 type sequence T description SECOND MALTOSE BINDING SITE. source : 26 21) chain A residue 599 type sequence A description SECOND MALTOSE BINDING SITE. source : 26 22) chain A residue 601 type sequence G description SECOND MALTOSE BINDING SITE. source : 26 23) chain A residue 603 type sequence N description SECOND MALTOSE BINDING SITE. source : 26 24) chain A residue 627 type sequence N description SECOND MALTOSE BINDING SITE. source : 26 25) chain A residue 628 type sequence Q description SECOND MALTOSE BINDING SITE. source : 26 26) chain A residue 633 type sequence Y description SECOND MALTOSE BINDING SITE. source : 26 27) chain A residue 301 type sequence Y description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 28) chain A residue 411 type sequence E description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 29) chain A residue 412 type sequence R description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 30) chain A residue 413 type sequence W description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 31) chain A residue 414 type sequence I description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 32) chain A residue 446 type sequence G description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 33) chain A residue 448 type sequence V description THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE. source : 36 34) chain A residue 227 type catalytic sequence R description 45 source MCSA : MCSA1 35) chain A residue 229 type catalytic sequence D description 45 source MCSA : MCSA1 36) chain A residue 257 type catalytic sequence Q description 45 source MCSA : MCSA1 37) chain A residue 327 type catalytic sequence H description 45 source MCSA : MCSA1 38) chain A residue 328 type catalytic sequence D description 45 source MCSA : MCSA1 39) chain A residue 229 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI1 40) chain A residue 257 type ACT_SITE sequence Q description Proton donor source Swiss-Prot : SWS_FT_FI2 41) chain A residue 145 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 42) chain A residue 190 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 193 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 199 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 45) chain A residue 227 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 46) chain A residue 232 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 47) chain A residue 233 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 48) chain A residue 315 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 49) chain A residue 327 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 50) chain A residue 371 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 51) chain A residue 375 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 52) chain A residue 577 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 53) chain A residue 51 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 54) chain A residue 53 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 55) chain A residue 100 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 56) chain A residue 139 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 57) chain A residue 140 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 58) chain A residue 27 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 59) chain A residue 29 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 60) chain A residue 32 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 61) chain A residue 33 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 62) chain A residue 328 type SITE sequence D description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI4

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