eF-site ID 4zwj-ABCD PDB Code 4zwj Chain A, B, C, D click to enlarge Title Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Classification SIGNALING PROTEIN Compound Chimera protein of human Rhodopsin, mouse S-arrestin, and T4 Endolysin Source Mus musculus (Mouse) (ARRS_MOUSE) Sequence A:  NIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNA AKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRML QQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP B:  MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP C:  NIFEMLRIDEGVITKDEAEKLFNQDVDAAVRGILRNAKLK PVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKR WDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYMCGT EGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYM FLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADL FMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLGGEIA LWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMA LACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFV IYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQ KAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQGSCFG PIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCG KNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGVVLVD PELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLYFSRV QVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPDYLPC SVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKIPKKS SVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLNLSVS LSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQIANVV LYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLLANNR ERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGILVSYH IKVKLTVSGFLTSSEVATEVPFRLMHPQP D:  NIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNA AKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRML QQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP Description Functional site 1) chain A residue 123-139 type prosite sequence IALWSLVVLAIERYVVV description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. IALwSLVVLAIERYVvV source prosite : PS00237 2) chain A residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 3) chain A residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 4) chain B residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 5) chain B residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 6) chain C residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 7) chain C residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 8) chain D residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 9) chain D residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 10) chain A residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI23 11) chain B residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI23 12) chain C residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI23 13) chain D residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI23 14) chain A residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI24 15) chain B residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI24 16) chain C residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI24 17) chain D residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI24 18) chain A residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI25 19) chain B residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI25 20) chain C residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI25 21) chain D residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI25 22) chain C residue 1011 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 1011 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 1011 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 1020 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2 26) chain D residue 1020 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 1032 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 1104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 1104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 30) chain D residue 1032 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 31) chain D residue 1104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 1117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 33) chain C residue 1132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 34) chain D residue 1117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 35) chain D residue 1132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 1117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 1132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 1-36 type TOPO_DOM sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 97-110 type TOPO_DOM sequence TSLHGYFVFGPTGC description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 40) chain A residue 174-202 type TOPO_DOM sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 275-284 type TOPO_DOM sequence IFTHQGSCFG description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 42) chain B residue 1-36 type TOPO_DOM sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 97-110 type TOPO_DOM sequence TSLHGYFVFGPTGC description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 44) chain B residue 174-202 type TOPO_DOM sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 45) chain B residue 275-284 type TOPO_DOM sequence IFTHQGSCFG description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 46) chain C residue 1-36 type TOPO_DOM sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 47) chain C residue 97-110 type TOPO_DOM sequence TSLHGYFVFGPTGC description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 48) chain C residue 174-202 type TOPO_DOM sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 49) chain C residue 275-284 type TOPO_DOM sequence IFTHQGSCFG description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 50) chain D residue 1-36 type TOPO_DOM sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 51) chain D residue 97-110 type TOPO_DOM sequence TSLHGYFVFGPTGC description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 52) chain D residue 174-202 type TOPO_DOM sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 53) chain D residue 275-284 type TOPO_DOM sequence IFTHQGSCFG description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI5 54) chain A residue 37-61 type TRANSMEM sequence FSMLAAYMFLLIVLGFPINFLTLYV description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI6 55) chain B residue 37-61 type TRANSMEM sequence FSMLAAYMFLLIVLGFPINFLTLYV description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI6 56) chain C residue 37-61 type TRANSMEM sequence FSMLAAYMFLLIVLGFPINFLTLYV description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI6 57) chain D residue 37-61 type TRANSMEM sequence FSMLAAYMFLLIVLGFPINFLTLYV description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI6 58) chain B residue 62-73 type TOPO_DOM sequence TVQHKKLRTPLN description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 59) chain B residue 134-152 type TOPO_DOM sequence ERYVVVCKPMSNFRFGENH description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 60) chain B residue 225-252 type TOPO_DOM sequence QLVFTVKEAAAQQQESATTQKAEKEVTR description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 61) chain C residue 62-73 type TOPO_DOM sequence TVQHKKLRTPLN description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 62) chain C residue 134-152 type TOPO_DOM sequence ERYVVVCKPMSNFRFGENH description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 63) chain C residue 225-252 type TOPO_DOM sequence QLVFTVKEAAAQQQESATTQKAEKEVTR description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 64) chain D residue 62-73 type TOPO_DOM sequence TVQHKKLRTPLN description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 65) chain D residue 134-152 type TOPO_DOM sequence ERYVVVCKPMSNFRFGENH description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 66) chain D residue 225-252 type TOPO_DOM sequence QLVFTVKEAAAQQQESATTQKAEKEVTR description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 67) chain A residue 62-73 type TOPO_DOM sequence TVQHKKLRTPLN description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 68) chain A residue 134-152 type TOPO_DOM sequence ERYVVVCKPMSNFRFGENH description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 69) chain A residue 225-252 type TOPO_DOM sequence QLVFTVKEAAAQQQESATTQKAEKEVTR description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI7 70) chain A residue 74-96 type TRANSMEM sequence YILLNLAVADLFMVLGGFTSTLY description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI8 71) chain B residue 74-96 type TRANSMEM sequence YILLNLAVADLFMVLGGFTSTLY description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI8 72) chain C residue 74-96 type TRANSMEM sequence YILLNLAVADLFMVLGGFTSTLY description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI8 73) chain D residue 74-96 type TRANSMEM sequence YILLNLAVADLFMVLGGFTSTLY description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI8 74) chain A residue 111-133 type TRANSMEM sequence NLQGFFATLGGEIALWSLVVLAI description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI9 75) chain B residue 111-133 type TRANSMEM sequence NLQGFFATLGGEIALWSLVVLAI description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI9 76) chain C residue 111-133 type TRANSMEM sequence NLQGFFATLGGEIALWSLVVLAI description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI9 77) chain D residue 111-133 type TRANSMEM sequence NLQGFFATLGGEIALWSLVVLAI description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI9 78) chain A residue 153-173 type TRANSMEM sequence AIMGVAFTWVMALACAAPPLA description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI10 79) chain B residue 153-173 type TRANSMEM sequence AIMGVAFTWVMALACAAPPLA description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI10 80) chain C residue 153-173 type TRANSMEM sequence AIMGVAFTWVMALACAAPPLA description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI10 81) chain D residue 153-173 type TRANSMEM sequence AIMGVAFTWVMALACAAPPLA description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI10 82) chain A residue 203-224 type TRANSMEM sequence FVIYMFVVHFTIPMIIIFFCYG description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI11 83) chain B residue 203-224 type TRANSMEM sequence FVIYMFVVHFTIPMIIIFFCYG description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI11 84) chain C residue 203-224 type TRANSMEM sequence FVIYMFVVHFTIPMIIIFFCYG description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI11 85) chain D residue 203-224 type TRANSMEM sequence FVIYMFVVHFTIPMIIIFFCYG description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI11 86) chain A residue 253-274 type TRANSMEM sequence MVIIYVIAFLICWVPYASVAFY description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI12 87) chain B residue 253-274 type TRANSMEM sequence MVIIYVIAFLICWVPYASVAFY description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI12 88) chain C residue 253-274 type TRANSMEM sequence MVIIYVIAFLICWVPYASVAFY description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI12 89) chain D residue 253-274 type TRANSMEM sequence MVIIYVIAFLICWVPYASVAFY description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI12 90) chain A residue 285-309 type TRANSMEM sequence PIFMTIPAFFAKSAAIYNPVIYIMM description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI13 91) chain B residue 285-309 type TRANSMEM sequence PIFMTIPAFFAKSAAIYNPVIYIMM description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI13 92) chain C residue 285-309 type TRANSMEM sequence PIFMTIPAFFAKSAAIYNPVIYIMM description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI13 93) chain D residue 285-309 type TRANSMEM sequence PIFMTIPAFFAKSAAIYNPVIYIMM description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI13 94) chain C residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 95) chain C residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 96) chain D residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 97) chain D residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 98) chain A residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 99) chain A residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 100) chain B residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 101) chain B residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 102) chain A residue 113 type SITE sequence Q description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343 source Swiss-Prot : SWS_FT_FI15 103) chain B residue 113 type SITE sequence Q description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343 source Swiss-Prot : SWS_FT_FI15 104) chain C residue 113 type SITE sequence Q description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343 source Swiss-Prot : SWS_FT_FI15 105) chain D residue 113 type SITE sequence Q description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343 source Swiss-Prot : SWS_FT_FI15 106) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 107) chain B residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 108) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 109) chain D residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 110) chain A residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 111) chain B residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 112) chain C residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 113) chain D residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 114) chain A residue 290-306 type prosite sequence IPAFFAKSAAIYNPVIY description OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKSAAiyNPviY source prosite : PS00238 115) chain A residue 2066-2084 type prosite sequence FRYGQEDIDVMGLTFRRDL description ARRESTINS Arrestins signature. FRYGqEDiDVMGLtFrRDL source prosite : PS00295 116) chain A residue 1011 type catalytic sequence E description 921 source MCSA : MCSA1 117) chain A residue 1020 type catalytic sequence D description 921 source MCSA : MCSA1 118) chain C residue 1011 type catalytic sequence E description 921 source MCSA : MCSA3 119) chain D residue 1011 type catalytic sequence E description 921 source MCSA : MCSA4 120) chain D residue 1020 type catalytic sequence D description 921 source MCSA : MCSA4

Display surface Download Links