eF-site ID 6cmo-ABGHLR PDB Code 6cmo Chain A, B, G, H, L, R click to enlarge Title Rhodopsin-Gi complex Classification SIGNALING PROTEIN Compound chimera protein of Soluble cytochrome b562 and Rhodopsin Source (6CMO) Sequence A:  MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLG AGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQS IIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLD RIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFD VGAQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM NRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKK SPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIY THFTCSTDTKNVQFVFDAVTDVIIKNNLKDCGLF B:  QSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPV GRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLI IWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTS SGDTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFV SGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSK SGRLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGV TDDGMAVATGSWDSFLKIWN G:  NTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAH AKEDPLLTPVPASENPFR H:  VQLVESGGGLVQPGGSLRLSCAASGFNFYYSSIHWVRQAP GKGLEWVASIYSYSGSTSYADSVKGRFTISADTSKNTAYL QMNSLRAEDTAVYYCARYPWYWWMEKPYLSLYGMDYWGQG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPS SSLGTQTYICNVNHKPSNTKVDKKVEPKSC L:  MTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKA PKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQPEDF ATYYCQQSSSSLITFGQGTKVEIKRTVAAPSVFIFPPSDS QLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESV TEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSS PVTKSFNRGEC R:  MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT ICC Description (1)  Soluble cytochrome b562,Rhodopsin, Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Fab light chain, Fab Heavy chain Functional site 1) chain A residue 269 type MOD_RES sequence N description N-acetylalanine => ECO:0000269|PubMed:7626050 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 2 type LIPID sequence G description N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805 source Swiss-Prot : SWS_FT_FI10 3) chain A residue 3 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824 source Swiss-Prot : SWS_FT_FI11 4) chain R residue 279 type LIPID sequence Q description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824 source Swiss-Prot : SWS_FT_FI11 5) chain R 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_FI12 6) chain R residue 296 type MOD_RES sequence K description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI13 7) chain R residue 322 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 8) chain R residue 323 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699 source Swiss-Prot : SWS_FT_FI14 9) chain R residue 15 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425 source Swiss-Prot : SWS_FT_FI15 10) chain A residue 181 type MOD_RES sequence T description Cysteine methyl ester => ECO:0000269|PubMed:1903391 source Swiss-Prot : SWS_FT_FI2 11) chain R residue 134-152 type LIPID sequence ERYVVVCKPMSNFRFGENH description S-geranylgeranyl cysteine => ECO:0000269|PubMed:12764189, ECO:0000269|PubMed:1903391, ECO:0000269|PubMed:7626050 source Swiss-Prot : SWS_FT_FI3 12) chain R residue 225-252 type LIPID sequence QLVFTVKEAAAQQQESATTQKAEKEVTR description S-geranylgeranyl cysteine => ECO:0000269|PubMed:12764189, ECO:0000269|PubMed:1903391, ECO:0000269|PubMed:7626050 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 200 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21115486 source Swiss-Prot : SWS_FT_FI5 14) chain R residue 174-202 type BINDING sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES description BINDING => ECO:0000269|PubMed:21115486 source Swiss-Prot : SWS_FT_FI5 15) chain R residue 275-284 type BINDING sequence IFTHQGSCFG description BINDING => ECO:0000269|PubMed:21115486 source Swiss-Prot : SWS_FT_FI5 16) chain A residue 326 type BINDING sequence S description BINDING => ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q source Swiss-Prot : SWS_FT_FI6 17) chain A residue 178 type MOD_RES sequence R description ADP-ribosylarginine; by cholera toxin => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 18) chain A residue 204 type MOD_RES sequence Q description Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704 source Swiss-Prot : SWS_FT_FI8 19) chain A residue 351 type MOD_RES sequence C description ADP-ribosylcysteine; by pertussis toxin => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 20) chain R residue 123-139 type prosite sequence IALWSLVVLAIERYVVV description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. IALwSLVVLAIERYVvV source prosite : PS00237 21) chain R residue 290-306 type prosite sequence IPAFFAKSAAIYNPVIY description OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKSAAiyNPviY source prosite : PS00238 22) chain B residue 70-84 type prosite sequence LVSASQDGKLIIWDS description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS source prosite : PS00678 23) chain B residue 157-171 type prosite sequence IVTSSGDTTCALWDI description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS source prosite : PS00678 24) chain B residue 285-299 type prosite sequence LLAGYDDFNCNVWDA description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS source prosite : PS00678 25) chain A residue 175 type BINDING sequence L description BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q source Swiss-Prot : SWS_FT_FI4 26) chain L residue 193-199 type prosite sequence YACEVTH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH source prosite : PS00290 27) chain H residue 212-218 type prosite sequence YICNVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH source prosite : PS00290

Display surface Download Links