› 5vex

X-ray diffraction
3Å resolution

Structure of the human GLP-1 receptor complex with NNC0640

Released:
DOI: 10.2210/pdb5vex/pdb
PDB entry 5vex coloured by chain, front view.
PDB entry 5vex coloured by chain, side view.
PDB entry 5vex coloured by chain, top view.
Source organisms:
Primary publication:
Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators.
Song G, Yang D, Wang Y, de Graaf C, Zhou Q, Jiang S, Liu K, Cai X, Dai A, Lin G, Liu D, Wu F, Wu Y, Zhao S, Ye L, Han GW, Lau J, Wu B, Hanson MA, Liu ZJ, Wang MW, Stevens RC
Nature 546 312-315 (2017)
PMID: 28514449

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin; Glucagon-like peptide 1 receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 52.59 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P43220 (Residues: 128-204, 206-206, 215-257, 261-431; Coverage: 66%)
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
Gene names: E, GLP1R
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 97V 2 x 97V
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P1
Unit cell:
a: 64.81Å b: 67.51Å c: 83.66Å
α: 91.55° β: 89.88° γ: 107.56°
R-values:
R R work R free
0.234 0.233 0.256
Expression system: Spodoptera frugiperda

Quick links

Citations

24 review citations

Glucagon-like peptide 1 (GLP-1).
Müller et al. (2019)
23 more

28 mentions without citation

G protein-coupled receptors: structure- and function-based drug discovery.
Yang et al. (2021)
27 more