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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

27XK

A cryo-EM structure of GLP1-Y11-GLP1R-Gs complex

Functional Information from PROSITE/UniProt
site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDeya.CWpdGepgsfvnvsCP
ChainResidueDetails
RCYS62-PRO86
site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLMVaILYCFvNneV
ChainResidueDetails
RGLN394-VAL409
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
BVAL327-GLY341
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues29
DetailsPeptide: {"description":"Glucagon-like peptide 1(7-36)","featureId":"PRO_0000011260","evidences":[{"source":"PubMed","id":"2753890","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P55095","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Arginine amide","evidences":[{"source":"PubMed","id":"2753890","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues42
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues51
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues3
DetailsRegion: {"description":"Important for allosteric inhibitor binding","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsSite: {"description":"Interaction with the endogenous ligand GLP-1","evidences":[{"source":"PubMed","id":"19861722","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"PubMed","id":"21901419","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine","evidences":[{"source":"PubMed","id":"21901419","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22412906","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

255900

PDB entries from 2026-07-01

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