eF-site ID 4zwj-D PDB Code 4zwj Chain 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 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 D residue 1011 type catalytic sequence E description 921 source MCSA : MCSA4 2) chain D residue 1020 type catalytic sequence D description 921 source MCSA : MCSA4 3) 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 4) 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 5) 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 6) chain D residue 1032 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 7) chain D residue 1104 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 8) chain D residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 9) chain D residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 10) chain D residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI22 11) chain D residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI23 12) chain D residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI24 13) chain D residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI25 14) chain D residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 15) chain D residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 16) 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 17) 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 18) 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 19) chain D residue 1117 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 20) chain D residue 1132 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 21) chain D residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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

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