› 6oba

X-ray diffraction
3.1Å resolution

The beta2 adrenergic receptor bound to a negative allosteric modulator

Released:
DOI: 10.2210/pdb6oba/pdb
PDB entry 6oba coloured by chain, front view.
PDB entry 6oba coloured by chain, side view.
PDB entry 6oba coloured by chain, top view.
Source organisms:
Primary publication:
An allosteric modulator binds to a conformational hub in the β2 adrenergic receptor.
Liu X, Kaindl J, Korczynska M, Stößel A, Dengler D, Stanek M, Hübner H, Clark MJ, Mahoney J, Matt RA, Xu X, Hirata K, Shoichet BK, Sunahara RK, Kobilka BK, Gmeiner P
Nat Chem Biol 16 749-755 (2020)
PMID: 32483378

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-112926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-2 adrenergic receptor; Endolysin Chain: A
Molecule details ›
Chain: A
Length: 500 amino acids
Theoretical weight: 56.6 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07550 (Residues: 1-230, 264-365; Coverage: 80%)
  • Canonical: D9IEF7 (Residues: 2-162; Coverage: 98%)
Gene names: ADRB2, ADRB2R, B2AR, T4Tp126, e
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand CLR 2 x CLR
Ligand JTZ 1 x JTZ
Ligand M3J 1 x M3J
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: P212121
Unit cell:
a: 40.46Å b: 75.71Å c: 173.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.251 0.277
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

A practical guide to large-scale docking.
Bender et al. (2021)
1 more

16 mentions without citation

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