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6LN2

Crystal structure of full length human GLP1 receptor in complex with Fab fragment (Fab7F38)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0004930molecular_functionG protein-coupled receptor activity
A0004967molecular_functionglucagon receptor activity
A0005506molecular_functioniron ion binding
A0007166biological_processcell surface receptor signaling pathway
A0007186biological_processG protein-coupled receptor signaling pathway
A0008528molecular_functionG protein-coupled peptide receptor activity
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0043448biological_processalkane catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
AILE1033-GLY1043

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
BTYR191-HIS197
CTYR206-HIS212

site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDeya.CWpdGepgsfvnvsCP
ChainResidueDetails
ACYS62-PRO86

site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLMVaILYCFvNneV
ChainResidueDetails
AGLN394-VAL409

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues53
DetailsDomain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues29
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues51
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues3
DetailsRegion: {"description":"Important for allosteric inhibitor binding","evidences":[{"source":"PubMed","id":"28514449","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsSite: {"description":"Interaction with the endogenous ligand GLP-1","evidences":[{"source":"PubMed","id":"19861722","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"PubMed","id":"21901419","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine","evidences":[{"source":"PubMed","id":"21901419","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22412906","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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