5OTU: Extracellular domain of GLP-1 receptor

Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Hcs. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Jul 2018.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,303
Mol. weight: 33.94 kDa
Released: 4 Jul 2018

Explore 5OTU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5OTU contains 16 α-helices and 20 β-strands across 4 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, 10 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
β-strand	75	1	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	112	1	4
α-helix	118	1
β-strand	119	1	4
α-helix	120	1
β-strand	122	1	3
α-helix	124-126	3

Chains B and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	13-33	21

Chain C: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	32-52	21
α-helix	54-56	3
β-strand	62	1	5
α-helix	63-64	2
β-strand	65-66	2	6
β-strand	71-72	2	6
β-strand	75	1	5
β-strand	79-84	6	7
α-helix	85-86	2
α-helix	92-94	3
β-strand	99-104	6	7
β-strand	110	1	7
β-strand	112	1	8
β-strand	119	1	8
β-strand	122	1	7
α-helix	124-126	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glucagon-like peptide 1 receptor	A, C	protein	116	Homo sapiens	P43220 (AlphaFold model)
Glucagon	B, D	protein	31	Homo sapiens	P01275 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>5OTU_1 Glucagon-like peptide 1 receptor (chains A, C)
RPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNV
SCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEE

Sequence of entity 2 (B, D), FASTA

>5OTU_2 Glucagon (chains B, D)
HXEGXFTSDVSSYLEGQAAKEFIAWLVKGRG

Primary citation

alpha-Helix or beta-Turn? An Investigation into N-Terminally Constrained Analogues of Glucagon-like Peptide 1 (GLP-1) and Exendin-4. Oddo, A., Mortensen, S., Thogersen, H. et al. Biochemistry (2018) 57:4148-4154. DOI 10.1021/acs.biochem.8b00105 · 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…
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
7RTB 2.14 Å, Peptide-19 bound to the Glucagon-Like Peptide-1 Receptor (GLP-1R)

Browse structure collections

About this viewer

MolViewer shows 5OTU 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.