eF-site ID 6nbh-ABGNPR PDB Code 6nbh Chain A, B, G, N, P, R click to enlarge Title Cryo-EM structure of parathyroid hormone receptor type 1 in complex with a long-acting parathyroid hormone analog and G protein Classification SIGNALING PROTEIN Compound Parathyroid hormone/parathyroid hormone-related peptide receptor Source (6NBH) Sequence A:  DQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGE SGKSTIVKQTGIFETKFQVDKVNFHMFDVGGQRDERRKWI QCFNDVTAIIFVVASSQTNRLQEALNLFKSIWNNRWLRTI SVILFLNKQDLLAEKVLAIEDYFPEFARYTTPEDATPEPG EDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDT ENIRRVFNDCRDIIQRMHLRQYELL B:  ELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGR IQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIW DSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICS IYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSG DTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSG ACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFA TGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSG RLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTD DGMAVATGSWDSFLKIWN G:  TASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHA KEDPLLTPVPASENPFR N:  QVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWVRQA PGKGLEWVSDISQSGASISYTGSVKGRFTISRDNAKNTLY LQMNSLKPEDTAVYYCARCPAPFTRDCFDVTSTTYAYRGQ GTQVTV P:  AVAEIQLMHQRAKWIQDARRRAFLHKLIAEIHTA R:  VMTKEEQIFLLHRAQAQCEKRLKEVLGRPCLPEWDHILCW PLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVP GHNRTWANYSECVKFLTNETREREVFDRLAMIYTVGYSVS LASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIF VKDAVLYSGATLTAAAGYAGCRVAVTFFLYFLATNYYWIL VEGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAVFVAVWV SVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFIN IVRVLATKLRETNATRQQYRKLLKSTLVLMPLFGVHYIVF MATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNG EVQAEIKKSWSRWTLALDF Description (1)  Parathyroid hormone/parathyroid hormone-related peptide receptor, Long-acting parathyroid hormone analog, Gs protein alpha subunit, 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, Nanobody-35 Functional site 1) chain R residue 322 type sequence W description binding site for residue CLR R 601 source : AC1 2) chain R residue 326 type sequence V description binding site for residue CLR R 601 source : AC1 3) chain R residue 422 type sequence I description binding site for residue CLR R 602 source : AC2 4) chain R residue 426 type sequence A description binding site for residue CLR R 602 source : AC2 5) chain R residue 428 type sequence P description binding site for residue CLR R 602 source : AC2 6) chain R residue 361 type sequence W description binding site for residue CLR R 603 source : AC3 7) chain R residue 428 type sequence P description binding site for residue CLR R 603 source : AC3 8) chain R residue 382 type sequence V description binding site for residue CLR R 604 source : AC4 9) chain R residue 279 type sequence A description binding site for residue CLR R 605 source : AC5 10) chain R residue 286 type sequence T description binding site for residue CLR R 605 source : AC5 11) chain R residue 358 type sequence N description binding site for residue CLR R 606 source : AC6 12) chain R residue 359 type sequence K description binding site for residue CLR R 606 source : AC6 13) chain R residue 291 type sequence F description binding site for residue CLR R 607 source : AC7 14) chain R residue 275 type sequence A description binding site for residue PLM R 608 source : AC8 15) chain R residue 278 type sequence Y description binding site for residue PLM R 608 source : AC8 16) chain R residue 108-132 type prosite sequence CLPEWDHILCWPLGAPGEVVAVPCP description G_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. ClpeWDhil.CWplGapgevvavpCP source prosite : PS00649 17) chain R residue 451-466 type prosite sequence QGFFVAIIYCFCNGEV description G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFFVaIIYCFcNgeV source prosite : PS00650 18) chain B residue 70-84 type prosite sequence LVSASQDGKLIIWDS description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS source prosite : PS00678 19) chain B residue 157-171 type prosite sequence IVTSSGDTTCALWDI description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS source prosite : PS00678 20) chain B residue 285-299 type prosite sequence LLAGYDDFNCNVWDA description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS source prosite : PS00678 21) chain A residue 47 type BINDING sequence G description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 223 type BINDING sequence D description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 292 type BINDING sequence N description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 366 type BINDING sequence A description BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641 source Swiss-Prot : SWS_FT_FI1 25) chain R residue 151 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI10 26) chain R residue 161 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI10 27) chain R residue 166 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI10 28) chain R residue 176 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI10 29) chain A residue 54 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 352 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI3 31) chain R residue 307-320 type MOD_RES sequence HSLIFMAFFSEKKY description Phosphoserine => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI3 32) chain R residue 383-409 type MOD_RES sequence RVLATKLRETNATRQQYRKLLKS description Phosphoserine => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 300 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092 source Swiss-Prot : SWS_FT_FI6 34) chain R residue 410-428 type TRANSMEM sequence TLVLMPLFGVHYIVFMATP description Helical; Name=6 => ECO:0000255 source Swiss-Prot : SWS_FT_FI8 35) chain R residue 441-463 type TRANSMEM sequence MHYEMLFNSFQGFFVAIIYCFCN description Helical; Name=7 => ECO:0000255 source Swiss-Prot : SWS_FT_FI9

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