6kjv

X-ray diffraction
2.8Å resolution

Structure of thermal-stabilised(M9) human GLP-1 receptor transmembrane domain

Released:
Primary publication:
Mutagenesis facilitated crystallization of GLP-1R.
IUCrJ 6 996-1006 (2019)
PMID: 31709055

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

Structure analysis Details

Assembly composition:
monomeric (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: 52.58 KDa
Source organisms: Expression system: Spodoptera aff. frugiperda 1 BOLD-2017
UniProt:
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
  • Canonical: P43220 (Residues: 128-204, 215-257, 261-431; Coverage: 66%)
Gene names: E, GLP1R
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P1
Unit cell:
a: 65.03Å b: 68.3Å c: 83.43Å
α: 91.53° β: 90.34° γ: 106.49°
R-values:
R R work R free
0.249 0.247 0.28
Expression system: Spodoptera aff. frugiperda 1 BOLD-2017