eF-site ID 2o7b-ABCDEFGH PDB Code 2o7b Chain A, B, C, D, E, F, G, H click to enlarge Title Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with coumarate Classification LYASE Compound Putative histidine ammonia-lyase Source Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) (Q3IWB0_RHOS4) Sequence A:  PKPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASE ARLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANL VHHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTI ARLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGD FLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAM TGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAAL SDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGD IGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELN AVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTV LAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQ VTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARL CREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKK LVQALREQFPPLETDRPLGQEIAALATHLLQQSPV B:  PKPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASE ARLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANL VHHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTI ARLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGD FLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAM TGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAAL SDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGD IGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELN AVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTV LAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQ VTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARL CREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKK LVQALREQFPPLETDRPLGQEIAALATHLLQQSPV C:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV D:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV E:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV F:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV G:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV H:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV Description Functional site 1) chain A residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 2) chain A residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 3) chain A residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 4) chain A residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 5) chain A residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 6) chain A residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 7) chain A residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 8) chain B residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 9) chain B residue 406 type sequence G description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 10) chain D residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 11) chain D residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 A 701 source : AC1 12) chain A residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 13) chain B residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 14) chain B residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 15) chain B residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 16) chain B residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 17) chain B residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 18) chain B residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 19) chain B residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 20) chain C residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 21) chain C residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 B 701 source : AC2 22) chain B residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 23) chain B residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 24) chain C residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 25) chain C residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 26) chain C residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 27) chain C residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 28) chain C residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 29) chain C residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 30) chain C residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 31) chain D residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 C 701 source : AC3 32) chain A residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 33) chain A residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 34) chain C residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 35) chain D residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 36) chain D residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 37) chain D residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 38) chain D residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 39) chain D residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 40) chain D residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 41) chain D residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 D 701 source : AC4 42) chain E residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 43) chain E residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 44) chain E residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 45) chain E residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 46) chain E residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 47) chain E residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 48) chain E residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 49) chain F residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 50) chain H residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 51) chain H residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 E 701 source : AC5 52) chain E residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 53) chain F residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 54) chain F residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 55) chain F residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 56) chain F residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 57) chain F residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 58) chain F residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 59) chain F residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 60) chain G residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 61) chain G residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 F 701 source : AC6 62) chain F residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 63) chain F residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 64) chain G residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 65) chain G residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 66) chain G residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 67) chain G residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 68) chain G residue 153 type sequence L description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 69) chain G residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 70) chain G residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 71) chain G residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 72) chain H residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 G 701 source : AC7 73) chain E residue 300 type sequence Y description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 74) chain E residue 303 type sequence R description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 75) chain G residue 405 type sequence M description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 76) chain H residue 60 type sequence Y description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 77) chain H residue 67 type sequence G description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 78) chain H residue 89 type sequence H description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 79) chain H residue 90 type sequence L description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 80) chain H residue 432 type sequence N description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 81) chain H residue 435 type sequence N description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 82) chain H residue 436 type sequence Q description BINDING SITE FOR RESIDUE HC4 H 701 source : AC8 83) chain A residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 84) chain E residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 85) chain F residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 86) chain F residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 87) chain G residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 88) chain G residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 89) chain H residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 90) chain H residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 91) chain A residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 92) chain B residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 93) chain B residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 94) chain C residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 95) chain C residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 96) chain D residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 97) chain D residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 98) chain E residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 99) chain A residue 145-163 type prosite sequence GTVGXDLTPLAHMVLCL description PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTVGASGDLtPLAhmvL source prosite : PS00488 100) chain A residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 101) chain D residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 102) chain D residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 103) chain D residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 104) chain E residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 105) chain E residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 106) chain E residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 107) chain F residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 108) chain F residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 109) chain F residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 110) chain G residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 111) chain A residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 112) chain G residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 113) chain G residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 114) chain H residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 115) chain H residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 116) chain H residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 117) chain A residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 118) chain B residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 119) chain B residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 120) chain B residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 121) chain C residue 89 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 122) chain C residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 123) chain C residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 124) chain A residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 125) chain B residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 126) chain C residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 127) chain D residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 128) chain E residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 129) chain F residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 130) chain G residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 131) chain H residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 132) chain A residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 133) chain B residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 134) chain C residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 135) chain D residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 136) chain E residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 137) chain F residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 138) chain G residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 139) chain H residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3

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