eF-site ID 5a11-B PDB Code 5a11 Chain B click to enlarge Title The crystal structure of Ta-TFP, a thiocyanate-forming protein involved in glucosinolate breakdown (space group P21) Classification IMMUNE SYSTEM Compound THIOCYANATE FORMING PROTEIN Source Thlaspi arvense (Field penny-cress) (G1FNI6_THLAR) Sequence B:  TLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDP PYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVA VGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKG GPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEA YNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFA TANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFE KPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSRE GFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGL LVHGGKLMTNERTDEMYFFAVNSST Description Functional site 1) chain B residue 157 type sequence R description BINDING SITE FOR RESIDUE IOD B 1349 source : AC2 2) chain B residue 80 type sequence R description BINDING SITE FOR RESIDUE IOD B 1350 source : AC3 3) chain B residue 94 type sequence R description BINDING SITE FOR RESIDUE IOD B 1351 source : AC6 4) chain B residue 148 type sequence K description BINDING SITE FOR RESIDUE IOD B 1351 source : AC6 5) chain B residue 94 type ACT_SITE sequence R description Proton donor => ECO:0000269|PubMed:26260516, ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 45 type SITE sequence Y description Essential for catalytic activity => ECO:0000269|PubMed:30900313 source Swiss-Prot : SWS_FT_FI10 7) chain B residue 154 type SITE sequence T description Critical for thiocyanate and epithionitrile formation with allylglucosinolate in the presence of myrosinase => ECO:0000269|PubMed:30900313 source Swiss-Prot : SWS_FT_FI11 8) chain B residue 157 type ACT_SITE sequence R description Proton donor => ECO:0000269|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 220 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI3 10) chain B residue 46 type BINDING sequence E description BINDING => ECO:0000305|PubMed:23999604 source Swiss-Prot : SWS_FT_FI4 11) chain B residue 310 type BINDING sequence V description BINDING => ECO:0000305|PubMed:23999604 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 94 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI5 13) chain B residue 266 type BINDING sequence E description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI5 14) chain B residue 270 type BINDING sequence D description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI5 15) chain B residue 274 type BINDING sequence H description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI5 16) chain B residue 129 type BINDING sequence T description BINDING => ECO:0000305|PubMed:28479247 source Swiss-Prot : SWS_FT_FI6 17) chain B residue 130 type BINDING sequence F description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI7 18) chain B residue 157 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI8 19) chain B residue 309 type BINDING sequence W description BINDING => ECO:0000305|PubMed:26260516, ECO:0000305|PubMed:28479247, ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI8 20) chain B residue 269 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:28479247 source Swiss-Prot : SWS_FT_FI9

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