3C59: Glucagon-like peptide 1 receptor

Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 19 Feb 2008.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,197
Mol. weight: 18.31 kDa
Ligands: 10M
Released: 19 Feb 2008

Explore 3C59 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3C59 contains 9 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	32-52	21
α-helix	54-56	3
β-strand	62	1	1
α-helix	63-64	2
β-strand	65-66	2	2
β-strand	71-72	2	2
α-helix	74	1
β-strand	75	1	1
α-helix	76	1
β-strand	79-84	6	3
α-helix	85-86	2
α-helix	92-94	3
β-strand	99-104	6	3
β-strand	110	1	3
β-strand	122	1	3
α-helix	124-126	3

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	10-27	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glucagon-like peptide 1 receptor	A	protein	122	Homo sapiens	P43220 (AlphaFold model)
Exendin-4	B	protein	31		P26349 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3C59_1 Glucagon-like peptide 1 receptor (chains A)
RPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNV
SCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLF
LY

Sequence of entity 2 (B), FASTA

>3C59_2 Exendin-4 (chains B)
DLSKQMEEEAVRMFIEWLKNGGPSSGAPPPS

Ligands and cofactors

ID	Name	Formula	Copies
10M	decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside	C22 H42 O10 S	1

Primary citation

Crystal Structure of the Ligand-bound Glucagon-like Peptide-1 Receptor Extracellular Domain. Runge, S., Thogersen, H., Madsen, K. et al. J Biol Chem (2008) 283:11340-11347. DOI 10.1074/jbc.M708740200 · PubMed

Other PDB entries of the same protein (UniProt P43220 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ZGM 1.8 Å, Crystal structure of Semaglutide peptide backbone in complex with the GLP-1 receptor…
5OTU 1.8 Å, Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Hcs
5OTT 1.92 Å, Extracellular domain of GLP-1 receptor in complex with exendin-4 variant Gly2Hcs/Thr5Hcs
5E94 2.0 Å, Antibody-bound Glucagon-like Peptide-1 receptor extracellular domain
5OTV 2.0 Å, Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cyc/Thr11Hcs
5OTX 2.0 Å, Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cys/Thr11Cys
3C5T 2.1 Å, Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular…
3IOL 2.1 Å, Crystal structure of Glucagon-Like Peptide-1 in complex with the extracellular domain of…
5OTW 2.1 Å, Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Cys
6X18 2.1 Å, GLP-1 peptide hormone bound to Glucagon-Like peptide-1 (GLP-1) Receptor
6X19 2.1 Å, Non peptide agonist CHU-128, bound to Glucagon-Like peptide-1 (GLP-1) Receptor
9NTU 2.1 Å, Cryo-EM structure of BETP-GLP-1(9-36)-GLP-1R-Gs complex

Browse structure collections

About this viewer

MolViewer shows 3C59 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.