eF-site ID 6nbh-R
PDB Code 6nbh
Chain R

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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 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 R
residue 151
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

19) chain R
residue 161
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

20) chain R
residue 166
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

21) chain R
residue 176
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

22) chain R
residue 307-320
type MOD_RES
sequence HSLIFMAFFSEKKY
description Phosphoserine => ECO:0000250|UniProtKB:P63092
source Swiss-Prot : SWS_FT_FI3

23) chain R
residue 383-409
type MOD_RES
sequence RVLATKLRETNATRQQYRKLLKS
description Phosphoserine => ECO:0000250|UniProtKB:P63092
source Swiss-Prot : SWS_FT_FI3

24) chain R
residue 410-428
type TRANSMEM
sequence TLVLMPLFGVHYIVFMATP
description Helical; Name=6 => ECO:0000255
source Swiss-Prot : SWS_FT_FI8

25) 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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