eF-site ID 4zwj-A PDB Code 4zwj Chain A 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 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 A residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI23 5) chain A residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI24 6) chain A residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI25 7) 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 8) 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 9) chain A residue 1032 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 1104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 1117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 1132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 13) 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 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) chain A residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 28) chain A residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 29) 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 30) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 31) chain A residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 32) chain A residue 290-306 type prosite sequence IPAFFAKSAAIYNPVIY description OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKSAAiyNPviY source prosite : PS00238 33) chain A residue 2066-2084 type prosite sequence FRYGQEDIDVMGLTFRRDL description ARRESTINS Arrestins signature. FRYGqEDiDVMGLtFrRDL source prosite : PS00295 34) chain A residue 1011 type catalytic sequence E description 921 source MCSA : MCSA1 35) chain A residue 1020 type catalytic sequence D description 921 source MCSA : MCSA1

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