eF-site ID 5a11-A PDB Code 5a11 Chain A 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 A:  TLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDP PYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVA VGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKG GPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEA YNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFA TANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFE KPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSRE GFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGL LVHGGKLMTNERTDEMYFFAVNSST Description Functional site 1) chain A residue 157 type sequence R description BINDING SITE FOR RESIDUE IOD A 1349 source : AC1 2) chain A residue 80 type sequence R description BINDING SITE FOR RESIDUE IOD A 1350 source : AC4 3) chain A residue 10 type sequence M description BINDING SITE FOR RESIDUE IOD A 1351 source : AC5 4) chain A 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 5) chain A 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 6) chain A residue 220 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:30900313 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 46 type BINDING sequence E description BINDING => ECO:0000305|PubMed:23999604 source Swiss-Prot : SWS_FT_FI4 8) chain A residue 310 type BINDING sequence V description BINDING => ECO:0000305|PubMed:23999604 source Swiss-Prot : SWS_FT_FI4 9) chain A 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 10) chain A 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 11) chain A 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 12) chain A 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 13) chain A residue 129 type BINDING sequence T description BINDING => ECO:0000305|PubMed:28479247 source Swiss-Prot : SWS_FT_FI6 14) chain A 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 15) chain A 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 16) chain A 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 17) chain A residue 269 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:28479247 source Swiss-Prot : SWS_FT_FI9 18) chain A residue 45 type SITE sequence Y description Essential for catalytic activity => ECO:0000269|PubMed:30900313 source Swiss-Prot : SWS_FT_FI10 19) chain A 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

Display surface Download Links