eF-site ID 1doc-A PDB Code 1doc Chain A click to enlarge Title THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS Classification OXIDOREDUCTASE Compound P-HYDROXYBENZOATE HYDROXYLASE Source Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (PHHY_PSEAE) Sequence A:  MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVL GRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATT VYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI YANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFW TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGR LFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFS QRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE Description Functional site 1) chain A residue 44 type sequence R description BINDING SITE FOR RESIDUE BR A 397 source : AC1 2) chain A residue 45 type sequence A description BINDING SITE FOR RESIDUE BR A 397 source : AC1 3) chain A residue 102 type sequence Q description BINDING SITE FOR RESIDUE BR A 397 source : AC1 4) chain A residue 103 type sequence T description BINDING SITE FOR RESIDUE BR A 397 source : AC1 5) chain A residue 214 type sequence R description BINDING SITE FOR RESIDUE BR A 397 source : AC1 6) chain A residue 293 type sequence P description BINDING SITE FOR RESIDUE BR A 398 source : AC2 7) chain A residue 297 type sequence K description BINDING SITE FOR RESIDUE BR A 398 source : AC2 8) chain A residue 298 type sequence G description BINDING SITE FOR RESIDUE BR A 398 source : AC2 9) chain A residue 297 type sequence K description BINDING SITE FOR RESIDUE BR A 519 source : AC3 10) chain A residue 335 type sequence R description BINDING SITE FOR RESIDUE BR A 519 source : AC3 11) chain A residue 388 type sequence L description BINDING SITE FOR RESIDUE BR A 519 source : AC3 12) chain A residue 8 type sequence I description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 13) chain A residue 9 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 14) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 15) chain A residue 12 type sequence P description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 16) chain A residue 13 type sequence S description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 17) chain A residue 31 type sequence L description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 18) chain A residue 32 type sequence E description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 19) chain A residue 33 type sequence R description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 20) chain A residue 42 type sequence R description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 21) chain A residue 44 type sequence R description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 22) chain A residue 45 type sequence A description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 23) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 24) chain A residue 47 type sequence V description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 25) chain A residue 102 type sequence Q description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 26) chain A residue 158 type sequence C description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 27) chain A residue 159 type sequence D description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 28) chain A residue 160 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 29) chain A residue 163 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 30) chain A residue 285 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 31) chain A residue 286 type sequence D description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 32) chain A residue 296 type sequence A description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 33) chain A residue 297 type sequence K description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 34) chain A residue 298 type sequence G description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 35) chain A residue 299 type sequence L description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 36) chain A residue 300 type sequence N description BINDING SITE FOR RESIDUE FAD A 395 source : AC4 37) chain A residue 44 type sequence R description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 38) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 39) chain A residue 201 type sequence Y description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 40) chain A residue 212 type sequence S description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 41) chain A residue 214 type sequence R description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 42) chain A residue 222 type sequence Y description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 43) chain A residue 293 type sequence P description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 44) chain A residue 294 type sequence T description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 45) chain A residue 296 type sequence A description BINDING SITE FOR RESIDUE PHB A 396 source : AC5 46) chain A residue 286 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 13 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 32 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 42 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 102 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 201 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 212 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 222 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 293 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 299 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 201 type SITE sequence Y description Important for catalytic activity => ECO:0000269|PubMed:8312276 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 385 type SITE sequence Y description Important for catalytic activity => ECO:0000269|PubMed:8312276 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 72 type catalytic sequence H description 131 source MCSA : MCSA1 59) chain A residue 201 type catalytic sequence Y description 131 source MCSA : MCSA1 60) chain A residue 293 type catalytic sequence P description 131 source MCSA : MCSA1 61) chain A residue 297 type catalytic sequence K description 131 source MCSA : MCSA1 62) chain A residue 385 type catalytic sequence Y description 131 source MCSA : MCSA1

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