eF-site ID 6net-A PDB Code 6net Chain A click to enlarge Title FAD-dependent monooxygenase TropB from T. stipitatus substrate complex Classification FLAVOPROTEIN Compound FAD-dependent monooxygenase tropB Source (TROPB_TALSN) Sequence A:  QPLSVGIVGGGIIGVILAAGLVRRGIDVKVFEQARGFREI GAGMAFTANAVRCMEMLDPAIVWALRSSGHQAEARDYLRW VDGYHESSKRLYQLDAGIRGFEACRRDQFLEALVKVLPEG IVECQKRLQKIHEKNETEKVTLEFADGTFAHVDCVIGADG IRSRVRQHLFGEDSPYSHPHYSHKFAFRGLITMENAISAL GEDKARTLNMHVGPNAHLIHYPVANETMVNIAAFVSDPEE WPLSLVGPATREEAMGYFANWNPGLRAVLGFMPENIDRWA MFDTYDYPAPFFSRGKICLVGDAAHAAVPHHGAGACIGIE DALCATVLLAEVFVSTRGKSSIVRNRAIAAAFGSFNAVRR VRAQWFVDSSRRVCDLYQQPEWADPQKRIKAENCFEEIKD RSHKIWHFDYNSMLQEAIEKYRHNMGS Description Functional site 1) chain A residue 55 type sequence A description binding site for residue KJY A 501 source : AC1 2) chain A residue 94 type sequence D description binding site for residue KJY A 501 source : AC1 3) chain A residue 96 type sequence L description binding site for residue KJY A 501 source : AC1 4) chain A residue 119 type sequence F description binding site for residue KJY A 501 source : AC1 5) chain A residue 121 type sequence A description binding site for residue KJY A 501 source : AC1 6) chain A residue 65 type sequence E description binding site for residue KJY A 502 source : AC2 7) chain A residue 18 type sequence V description binding site for residue FAD A 503 source : AC3 8) chain A residue 19 type sequence G description binding site for residue FAD A 503 source : AC3 9) chain A residue 21 type sequence G description binding site for residue FAD A 503 source : AC3 10) chain A residue 22 type sequence I description binding site for residue FAD A 503 source : AC3 11) chain A residue 23 type sequence I description binding site for residue FAD A 503 source : AC3 12) chain A residue 41 type sequence F description binding site for residue FAD A 503 source : AC3 13) chain A residue 42 type sequence E description binding site for residue FAD A 503 source : AC3 14) chain A residue 43 type sequence Q description binding site for residue FAD A 503 source : AC3 15) chain A residue 48 type sequence R description binding site for residue FAD A 503 source : AC3 16) chain A residue 54 type sequence M description binding site for residue FAD A 503 source : AC3 17) chain A residue 55 type sequence A description binding site for residue FAD A 503 source : AC3 18) chain A residue 124 type sequence R description binding site for residue FAD A 503 source : AC3 19) chain A residue 144 type sequence K description binding site for residue FAD A 503 source : AC3 20) chain A residue 145 type sequence R description binding site for residue FAD A 503 source : AC3 21) chain A residue 146 type sequence L description binding site for residue FAD A 503 source : AC3 22) chain A residue 176 type sequence A description binding site for residue FAD A 503 source : AC3 23) chain A residue 177 type sequence D description binding site for residue FAD A 503 source : AC3 24) chain A residue 178 type sequence G description binding site for residue FAD A 503 source : AC3 25) chain A residue 182 type sequence R description binding site for residue FAD A 503 source : AC3 26) chain A residue 206 type sequence R description binding site for residue FAD A 503 source : AC3 27) chain A residue 321 type sequence G description binding site for residue FAD A 503 source : AC3 28) chain A residue 322 type sequence D description binding site for residue FAD A 503 source : AC3 29) chain A residue 332 type sequence G description binding site for residue FAD A 503 source : AC3 30) chain A residue 333 type sequence A description binding site for residue FAD A 503 source : AC3 31) chain A residue 334 type sequence G description binding site for residue FAD A 503 source : AC3 32) chain A residue 335 type sequence A description binding site for residue FAD A 503 source : AC3 33) chain A residue 336 type sequence C description binding site for residue FAD A 503 source : AC3 34) chain A residue 329 type sequence P description binding site for residue CL A 504 source : AC4 35) chain A residue 333 type sequence A description binding site for residue CL A 504 source : AC4 36) chain A residue 334 type sequence G description binding site for residue CL A 504 source : AC4 37) chain A residue 91 type sequence E description binding site for residue GOL B 2202 source : AC6 38) chain A residue 206 type ACT_SITE sequence R description ACT_SITE => ECO:0000269|PubMed:31346489 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 239 type ACT_SITE sequence Y description ACT_SITE => ECO:0000269|PubMed:31346489 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 12-32 type TRANSMEM sequence PLSVGIVGGGIIGVILAAGLV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 42 type BINDING sequence E description BINDING => ECO:0000269|PubMed:31346489, ECO:0000312|PDB:6NET, ECO:0000312|PDB:6NEU, ECO:0007744|PDB:6NES, ECO:0007744|PDB:6NEV source Swiss-Prot : SWS_FT_FI3 42) chain A residue 55 type BINDING sequence A description BINDING => ECO:0000269|PubMed:31346489, ECO:0000312|PDB:6NET, ECO:0000312|PDB:6NEU, ECO:0007744|PDB:6NES, ECO:0007744|PDB:6NEV source Swiss-Prot : SWS_FT_FI3 43) chain A residue 124 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31346489, ECO:0000312|PDB:6NET, ECO:0000312|PDB:6NEU, ECO:0007744|PDB:6NES, ECO:0007744|PDB:6NEV source Swiss-Prot : SWS_FT_FI3 44) chain A residue 322 type BINDING sequence D description BINDING => ECO:0000269|PubMed:31346489, ECO:0000312|PDB:6NET, ECO:0000312|PDB:6NEU, ECO:0007744|PDB:6NES, ECO:0007744|PDB:6NEV source Swiss-Prot : SWS_FT_FI3 45) chain A residue 335 type BINDING sequence A description BINDING => ECO:0000269|PubMed:31346489, ECO:0007744|PDB:6NES, ECO:0007744|PDB:6NEV source Swiss-Prot : SWS_FT_FI4 46) chain A residue 153 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 243 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI5

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