eF-site ID 3pwq-ABCDEFGHIJKR PDB Code 3pwq Chain A, B, C, D, E, F, G, H, I, J, K, R click to enlarge Title The Phenylacetyl-CoA monooxygenase PaaAC subcomplex Classification OXIDOREDUCTASE Compound Phenylacetic acid degradation protein paaC Source Escherichia coli (strain K12) (PAAA_ECOLI) Sequence A:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQYLQ RVLPGQQW B:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQYLQ RVLPGQQW C:  STQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAH SEIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLY SAAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGV IGWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQR QGFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNSA RSLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDLH FDTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKAW EEGTWVREAALAHAQK D:  STQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAH SEIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLY SAAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGV IGWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQR QGFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNNS ARSLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDL HFDTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKA WEEGTWVREAALAHAQK E:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQYLQ RVLPGQQW F:  STQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAH SEIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLY SAAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGV IGWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQR QGFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNSA RSLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDLH FDTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKAW EEGTWVREAALAHAQKQHARK G:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQYLQ RVLPGQQW H:  TQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAHS EIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLYS AAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGVI GWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQRQ GFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNSAR SLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDLHF DTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKAWE EGTWVREAALAHAQK I:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQY J:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQY K:  TAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALANIGLD LLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNLLLVE QPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLAAISA KAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAINKLWR FTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVFAGIN EATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQY R:  SNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALAN IGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNL LLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLA AISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAIN KLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVF AGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQY Description Functional site 1) chain C residue 33 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 2) chain D residue 37 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 3) chain D residue 103 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 193 type BINDING sequence M description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 6) chain D residue 214 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 7) chain D residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 8) chain F residue 33 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 9) chain F residue 37 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 10) chain F residue 103 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 11) chain C residue 37 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 12) chain F residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 13) chain F residue 193 type BINDING sequence M description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 14) chain F residue 214 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 15) chain F residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 16) chain H residue 33 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 17) chain H residue 37 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 18) chain H residue 103 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 19) chain H residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 20) chain H residue 193 type BINDING sequence M description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 103 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 22) chain H residue 214 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 23) chain H residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 25) chain C residue 193 type BINDING sequence M description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 214 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 27) chain C residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 33 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21247899 source Swiss-Prot : SWS_FT_FI1

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