eF-site ID 4z2h-A PDB Code 4z2h Chain A click to enlarge Title Serratia marcescens Chitinase B complexed with macrolide inhibitor 29 Classification HYDROLASE/HYDROLASE INHIBITOR Compound Chitinase B Source (CHIB_SERMA) Sequence A:  STRKAVIGYYFIPTNQINNYTETDTSVVPFPVSNITPAKA KQLTHINFSFLDINSNLECAWDPATNDAKARDVVNRLTAL KAHNPSLRIMFSIGGWYYSNDLGVSHANYVNAVKTPAART KFAQSCVRIMKDYGFDGVDIDWEYPQAAEVDGFIAALQEI RTLLNQQTIADGRQALPYQLTIAGAGGAFFLSRYYSKLAQ IVAPLDYINLMTYDLAGPWEKITNHQAALFGDAAGPTFYN ALREANLGWSWEELTRAFPSPFSLTVDAAVQQHLMMEGVP SAKIVMGVPFYGRAFKGVSGGNGGQYSSHSTPGEDPYPNA DYWLVGCDECVRDKDPRIASYRQLEQMLQGNYGYQRLWND KTKTPYLYHAQNGLFVTYDDAESFKYKAKYIKQQQLGGVM FWHLGQDNRNGDLLAALDRYFNAADYDDSQLDMGTGLRYT GVGPGNLPIMTAPAYVPGTTYAQGALVSYQGYVWQTKWGY ITSAPGSDSAWLKVGRLA Description Functional site 1) chain A residue 10 type sequence Y description binding site for residue M6A A 501 source : AC1 2) chain A residue 12 type sequence F description binding site for residue M6A A 501 source : AC1 3) chain A residue 51 type sequence F description binding site for residue M6A A 501 source : AC1 4) chain A residue 96 type sequence G description binding site for residue M6A A 501 source : AC1 5) chain A residue 97 type sequence W description binding site for residue M6A A 501 source : AC1 6) chain A residue 142 type sequence D description binding site for residue M6A A 501 source : AC1 7) chain A residue 144 type sequence E description binding site for residue M6A A 501 source : AC1 8) chain A residue 212 type sequence M description binding site for residue M6A A 501 source : AC1 9) chain A residue 214 type sequence Y description binding site for residue M6A A 501 source : AC1 10) chain A residue 215 type sequence D description binding site for residue M6A A 501 source : AC1 11) chain A residue 292 type sequence Y description binding site for residue M6A A 501 source : AC1 12) chain A residue 316 type sequence D description binding site for residue M6A A 501 source : AC1 13) chain A residue 339 type sequence I description binding site for residue M6A A 501 source : AC1 14) chain A residue 403 type sequence W description binding site for residue M6A A 501 source : AC1 15) chain A residue 12 type sequence F description binding site for residue GOL A 502 source : AC2 16) chain A residue 13 type sequence I description binding site for residue GOL A 502 source : AC2 17) chain A residue 14 type sequence P description binding site for residue GOL A 502 source : AC2 18) chain A residue 15 type sequence T description binding site for residue GOL A 502 source : AC2 19) chain A residue 51 type sequence F description binding site for residue GOL A 502 source : AC2 20) chain A residue 99 type sequence Y description binding site for residue GOL A 502 source : AC2 21) chain A residue 260 type sequence P description binding site for residue GOL A 503 source : AC3 22) chain A residue 263 type sequence F description binding site for residue GOL A 503 source : AC3 23) chain A residue 264 type sequence S description binding site for residue GOL A 503 source : AC3 24) chain A residue 439 type sequence R description binding site for residue GOL A 503 source : AC3 25) chain A residue 440 type sequence Y description binding site for residue GOL A 503 source : AC3 26) chain A residue 441 type sequence T description binding site for residue GOL A 503 source : AC3 27) chain A residue 244 type sequence R description binding site for residue GOL A 504 source : AC4 28) chain A residue 252 type sequence W description binding site for residue GOL A 504 source : AC4 29) chain A residue 259 type sequence F description binding site for residue GOL A 504 source : AC4 30) chain A residue 260 type sequence P description binding site for residue GOL A 504 source : AC4 31) chain A residue 261 type sequence S description binding site for residue GOL A 504 source : AC4 32) chain A residue 4 type sequence R description binding site for residue GOL A 505 source : AC5 33) chain A residue 46 type sequence H description binding site for residue GOL A 505 source : AC5 34) chain A residue 89 type sequence R description binding site for residue GOL A 505 source : AC5 35) chain A residue 162 type sequence R description binding site for residue GOL A 506 source : AC6 36) chain A residue 204 type sequence A description binding site for residue GOL A 506 source : AC6 37) chain A residue 207 type sequence D description binding site for residue GOL A 506 source : AC6 38) chain A residue 284 type sequence K description binding site for residue GOL A 506 source : AC6 39) chain A residue 323 type sequence Y description binding site for residue GOL A 507 source : AC7 40) chain A residue 325 type sequence L description binding site for residue GOL A 507 source : AC7 41) chain A residue 326 type sequence V description binding site for residue GOL A 507 source : AC7 42) chain A residue 327 type sequence G description binding site for residue GOL A 507 source : AC7 43) chain A residue 328 type sequence C description binding site for residue GOL A 507 source : AC7 44) chain A residue 329 type sequence D description binding site for residue GOL A 507 source : AC7 45) chain A residue 89 type sequence R description binding site for residue CL A 508 source : AC8 46) chain A residue 68 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 95 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 145 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 212 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 403 type BINDING sequence W description BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 144 type ACT_SITE sequence E description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 136-144 type prosite sequence FDGVDIDWE description GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDIDwE source prosite : PS01095

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