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› 5yqz

X-ray diffraction
3Å resolution

Structure of the glucagon receptor in complex with a glucagon analogue

Released:
DOI: 10.2210/pdb5yqz/pdb
Model geometry
Fit model/data
PDB entry 5yqz coloured by chain, front view.
PDB entry 5yqz coloured by chain, side view.
PDB entry 5yqz coloured by chain, top view.
Source organisms:
Primary publication:
Structure of the glucagon receptor in complex with a glucagon analogue.
Zhang H, Qiao A, Yang L, Van Eps N, Frederiksen KS, Yang D, Dai A, Cai X, Zhang H, Yi C, Cao C, He L, Yang H, Lau J, Ernst OP, Hanson MA, Stevens RC, Wang MW, Reedtz-Runge S, Jiang H, Zhao Q, Wu B
Nature 553 106-110 (2018)
PMID: 29300013

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid andN-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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132993 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Endolysin; Glucagon receptor Chain: R
Molecule details ›
Chain: R
Length: 575 amino acids
Theoretical weight: 65.8 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P47871 (Residues: 27-257, 260-432; Coverage: 89%)
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
Gene names: E, GCGR
Sequence domains:
Glucagon Chain: P
Molecule details ›
Chain: P
Length: 28 amino acids
Theoretical weight: 3.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01275 (Residues: 54-81; Coverage: 18%)
Gene name: GCG
Sequence domains: Peptide hormone

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand OLC 6 x OLC
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 60.12Å b: 108.79Å c: 216.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.232 0.261
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

14 review citations

Mechanisms of signalling and biased agonism in G protein-coupled receptors.
Wootten et al. (2018)
13 more

29 mentions without citation

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