eF-site ID 2o7e-ABCDEFGH PDB Code 2o7e Chain A, B, C, D, E, F, G, H click to enlarge Title Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to 2-aminoindan-2-phosphonic acid 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 VHFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTI ARLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGD FLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAM TGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAAL SDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGD IGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELN AVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTV LAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQ VTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARL CREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKK LVQALREQFPPLETDRPLGQEIAALATHLLQQSPV B:  PKPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASE ARLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANL VHFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTI ARLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGD FLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAM TGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAAL SDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGD IGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELN AVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTV LAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQ VTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARL CREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKK LVQALREQFPPLETDRPLGQEIAALATHLLQQSPV C:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV D:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV E:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV F:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV G:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL VQALREQFPPLETDRPLGQEIAALATHLLQQSPV H:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV HFLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA 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 PMI A 701 source : AC1 2) chain A residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 3) chain A residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 4) chain A residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 5) chain A residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 6) chain B residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 7) chain D residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 8) chain D residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 9) chain D residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI A 701 source : AC1 10) chain A residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 11) chain B residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 12) chain B residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 13) chain B residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 14) chain B residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 15) chain B residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 16) chain C residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 17) chain C residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 18) chain C residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI B 701 source : AC2 19) chain B residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 20) chain B residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 21) chain B residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 22) chain C residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 23) chain C residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 24) chain C residue 153 type sequence L description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 25) chain C residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 26) chain C residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 27) chain C residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 28) chain D residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI C 701 source : AC3 29) chain A residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 30) chain A residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 31) chain A residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 32) chain C residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 33) chain D residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 34) chain D residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 35) chain D residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 36) chain D residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 37) chain D residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI D 701 source : AC4 38) chain E residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 39) chain E residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 40) chain E residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 41) chain E residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 42) chain E residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 43) chain F residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 44) chain H residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 45) chain H residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 46) chain H residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI E 701 source : AC5 47) chain E residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 48) chain F residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 49) chain F residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 50) chain F residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 51) chain F residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 52) chain F residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 53) chain G residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 54) chain G residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 55) chain G residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI F 701 source : AC6 56) chain F residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 57) chain F residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 58) chain F residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 59) chain G residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 60) chain G residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 61) chain G residue 153 type sequence L description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 62) chain G residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 63) chain G residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 64) chain G residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 65) chain H residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI G 701 source : AC7 66) chain E residue 297 type sequence Q description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 67) chain E residue 300 type sequence Y description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 68) chain E residue 303 type sequence R description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 69) chain G residue 405 type sequence M description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 70) chain H residue 60 type sequence Y description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 71) chain H residue 149 type sequence X description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 72) chain H residue 203 type sequence N description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 73) chain H residue 333 type sequence N description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 74) chain H residue 350 type sequence F description BINDING SITE FOR RESIDUE PMI H 701 source : AC8 75) chain A residue 145-163 type prosite sequence GTVGXDLTPLAHMVLCL description PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTVGASGDLtPLAhmvL source prosite : PS00488 76) chain A residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 77) chain D residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 78) chain D residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 79) chain D residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 80) chain E residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 81) chain E residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 82) chain E residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 83) chain F residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 84) chain F residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 85) chain F residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 86) chain G residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 87) chain A residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 88) chain G residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 89) chain G residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 90) chain H residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 91) chain H residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 92) chain H residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 93) chain A residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 94) chain B residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 95) chain B residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 96) chain B residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 97) chain C residue 89 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 98) chain C residue 305 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 99) chain C residue 434 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2 100) chain A residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 101) chain B residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 102) chain C residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 103) chain D residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 104) chain E residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 105) chain F residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 106) chain G residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 107) chain H residue 60 type ACT_SITE sequence Y description Proton donor/acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 108) chain A residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 109) chain B residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 110) chain C residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 111) chain D residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 112) chain E residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 113) chain F residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 114) chain G residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 115) chain H residue 152 type MOD_RES sequence D description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI3 116) chain A residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 117) chain E residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 118) chain F residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 119) chain F residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 120) chain G residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 121) chain G residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 122) chain H residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 123) chain H residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 124) chain A residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 125) chain B residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 126) chain B residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 127) chain C residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 128) chain C residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 129) chain D residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 130) chain D residue 153 type CROSSLNK sequence L description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4 131) chain E residue 149 type CROSSLNK sequence X description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228 source Swiss-Prot : SWS_FT_FI4

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