eF-site ID 5w0p-D PDB Code 5w0p Chain D click to enlarge Title Crystal structure of rhodopsin bound to visual arrestin determined by X-ray free electron laser Classification SIGNALING PROTEIN Compound Endolysin,Rhodopsin,S-arrestin Source (ARRS_MOUSE) Sequence D:  RGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFT NSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRT GTWDAYMCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEP WQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNY ILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQG FFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAI MGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTL KPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAA AQQQESATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFY IFTHQGSCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFR NCMLTTICCGDDEASATVXKTETSVIFKKVSRDKSVTIYL GKRDYVDHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFR YGQEDIDVMGLTFRRDLYFSRVQVYPPVGAMSVLTQLQES LLKKLGDNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVD FEVKAFASDITDPEEDKIPKKSSVRLLIRKVQHAPPEMGP QPSAEASWQFFMSDKPLNLSVSLSKEIYFHGEPIPVTVTV TNNTDKVVKKIKVSVEQIANVVLYSSDYYVKPVASEETQE KVQPNSTLTKTLVLVPLLANNRERRGIALDGKIKHEDTNL ASSTIIKEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSE VATEVPFRLMHPQP Description Functional site 1) 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_FI1 2) 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_FI1 3) 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_FI1 4) 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_FI1 5) chain D residue 201 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI10 6) chain D residue 279 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI10 7) 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_FI11 8) chain D residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI12 9) chain D residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI13 10) chain D residue 334 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI14 11) chain D residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI14 12) chain D residue 336 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI15 13) chain D residue 340 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 14) chain D residue 342 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI16 15) chain D residue 343 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI17 16) chain D residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI18 17) chain D residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI18 18) chain D residue 2 type CARBOHYD sequence C description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI19 19) 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_FI2 20) chain D residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI20 21) chain D residue 2231 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P15887 source Swiss-Prot : SWS_FT_FI21 22) chain D residue -57 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI24 23) chain D residue -44 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI25 24) chain D residue -29 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI25 25) 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_FI3 26) 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_FI3 27) 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_FI3 28) 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_FI4 29) 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_FI5 30) 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_FI6 31) 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_FI7 32) 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_FI8 33) 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_FI9

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