eF-site ID 1e6q-M PDB Code 1e6q Chain M click to enlarge Title MYROSINASE FROM SINAPIS ALBA with the bound transition state analogue gluco-tetrazole Classification HYDROLASE Compound MYROSINASE MA1 Source ORGANISM_COMMON: WHITE MUSTARD; ORGANISM_SCIENTIFIC: SINAPIS ALBA; Sequence M:  EITCQENLPFTCGNTDALNSSSFSSDFIFGVASSAYQIEG TIGRGLNIWDGFTHRYPNKSGPDHGNGDTTCDSFSYWQKD IDVLDELNATGYRFSIAWSRIIPRGKRSRGVNEKGIDYYH GLISGLIKKGITPFVTLFHWDLPQTLQDEYEGFLDPQIID DFKDYADLCFEEFGDSVKYWLTINQLYSVPTRGYGSALDA PGRCSPTVDPSCYAGNSSTEPYIVAHHQLLAHAKVVDLYR KNYTHQGGKIGPTMITRWFLPYNDTDRHSIAATERMKEFF LGWFMGPLTNGTYPQIMIDTVGERLPSFSPEESNLVKGSY DFLGLNYYFTQYAQPSPNPVNSTNHTAMMDAGAKLTYINA SGHYIGPLFEKDKADSTDNIYYYPKGIYSVMDYFKNKYYN PLIYVTENGISTPGDENRNQSMLDYTRIDYLCSHLCFLNK VIKEKDVNVKGYLAWALGDNYEFNKGFTVRFGLSYIDWNN VTDRDLKKSGQWYQSFISP Description Functional site 1) chain M residue 95 type catalytic sequence R description 460 source MCSA : MCSA1 2) chain M residue 187 type catalytic sequence Q description 460 source MCSA : MCSA1 3) chain M residue 190 type catalytic sequence S description 460 source MCSA : MCSA1 4) chain M residue 328 type catalytic sequence N description 460 source MCSA : MCSA1 5) chain M residue 330 type catalytic sequence Y description 460 source MCSA : MCSA1 6) chain M residue 409 type catalytic sequence E description 460 source MCSA : MCSA1 7) chain M residue 187 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10978344 source Swiss-Prot : SWS_FT_FI3 8) chain M residue 259 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10978344 source Swiss-Prot : SWS_FT_FI3 9) chain M residue 330 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 10) chain M residue 457 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 11) chain M residue 464 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 12) chain M residue 21 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 13) chain M residue 60 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 14) chain M residue 361 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 15) chain M residue 482 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 16) chain M residue 90 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 17) chain M residue 218 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 18) chain M residue 244 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 19) chain M residue 265 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 20) chain M residue 292 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 21) chain M residue 343 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 22) chain M residue 346 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10978344, ECO:0000269|PubMed:15889170, ECO:0000269|PubMed:9195886 source Swiss-Prot : SWS_FT_FI5 23) chain M residue 405-413 type prosite sequence IYVTENGIS description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYVTENGIS source prosite : PS00572 24) chain M residue 29-43 type prosite sequence FIFGVASSAYQIEGT description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGvAsSAYQiEgT source prosite : PS00653 25) chain M residue 409 type ACT_SITE sequence E description Nucleophile source Swiss-Prot : SWS_FT_FI1 26) chain M residue 39 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 27) chain M residue 56 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 28) chain M residue 70 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 29) chain M residue 141 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 30) chain M residue 186 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2

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