eF-site ID 6cbq-AB PDB Code 6cbq Chain A, B click to enlarge Title Crystal structure of QscR bound to agonist S3 Classification transcription/agonist Compound LuxR family transcriptional regulator Source (Q9RMS5_PSEAI) Sequence A:  EREGYLEILSRITTEEEFFSLVLEICGNYGFEFFSFGARA PFPLTAPKYHFLSNYPGEWKSRYISEDYTSIDPIVRHGLL EYTPLIWNGEDFQENRFFWEEALHHGIRHGWSIPVRGKYG LISMLSLVRSSESIAATEILEKESFLLWITSMLQATFGDL LAPRIVPESNVRLTARETEMLKWTAVGKTYGEIGLILSID QRTVKFHIVNAMRKLNSSNKAEATMKAYAIGLLN B:  EREGYLEILSRITTEEEFFSLVLEICGNYGFEFFSFGARA PFPLTAPKYHFLSNYPGEWKSRYISEDYTSIDPIVRHGLL EYTPLIWNGEDFQENRFFWEEALHHGIRHGWSIPVRGKYG LISMLSLVRSSESIAATEILEKESFLLWITSMLQATFGDL LAPRIVPESNVRLTARETEMLKWTAVGKTYGEIGLILSID QRTVKFHIVNAMRKLNSSNKAEATMKAYAIGLLN Description Functional site 1) chain A residue 38 type sequence S description binding site for residue EVY A 301 source : AC1 2) chain A residue 40 type sequence G description binding site for residue EVY A 301 source : AC1 3) chain A residue 54 type sequence F description binding site for residue EVY A 301 source : AC1 4) chain A residue 56 type sequence S description binding site for residue EVY A 301 source : AC1 5) chain A residue 58 type sequence Y description binding site for residue EVY A 301 source : AC1 6) chain A residue 62 type sequence W description binding site for residue EVY A 301 source : AC1 7) chain A residue 66 type sequence Y description binding site for residue EVY A 301 source : AC1 8) chain A residue 75 type sequence D description binding site for residue EVY A 301 source : AC1 9) chain A residue 77 type sequence I description binding site for residue EVY A 301 source : AC1 10) chain A residue 78 type sequence V description binding site for residue EVY A 301 source : AC1 11) chain A residue 81 type sequence G description binding site for residue EVY A 301 source : AC1 12) chain A residue 101 type sequence F description binding site for residue EVY A 301 source : AC1 13) chain A residue 102 type sequence W description binding site for residue EVY A 301 source : AC1 14) chain A residue 125 type sequence I description binding site for residue EVY A 301 source : AC1 15) chain A residue 127 type sequence M description binding site for residue EVY A 301 source : AC1 16) chain B residue 38 type sequence S description binding site for residue EVY B 301 source : AC2 17) chain B residue 40 type sequence G description binding site for residue EVY B 301 source : AC2 18) chain B residue 54 type sequence F description binding site for residue EVY B 301 source : AC2 19) chain B residue 56 type sequence S description binding site for residue EVY B 301 source : AC2 20) chain B residue 58 type sequence Y description binding site for residue EVY B 301 source : AC2 21) chain B residue 62 type sequence W description binding site for residue EVY B 301 source : AC2 22) chain B residue 66 type sequence Y description binding site for residue EVY B 301 source : AC2 23) chain B residue 75 type sequence D description binding site for residue EVY B 301 source : AC2 24) chain B residue 77 type sequence I description binding site for residue EVY B 301 source : AC2 25) chain B residue 78 type sequence V description binding site for residue EVY B 301 source : AC2 26) chain B residue 81 type sequence G description binding site for residue EVY B 301 source : AC2 27) chain B residue 82 type sequence L description binding site for residue EVY B 301 source : AC2 28) chain B residue 102 type sequence W description binding site for residue EVY B 301 source : AC2 29) chain B residue 110 type sequence I description binding site for residue EVY B 301 source : AC2 30) chain B residue 125 type sequence I description binding site for residue EVY B 301 source : AC2 31) chain B residue 127 type sequence M description binding site for residue EVY B 301 source : AC2 32) chain B residue 129 type sequence S description binding site for residue EVY B 301 source : AC2 33) chain A residue 190-217 type prosite sequence GKTYGEIGLILSIDQRTVKFHIVNAMRK description HTH_LUXR_1 LuxR-type HTH domain signature. GktYgeIGliLsIdqrTVkfHivNAmrK source prosite : PS00622

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