X-ray diffraction
3.5Å resolution

Structure of a nanobody-stabilized active state of the beta2 adrenoceptor


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:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-2 adrenergic receptor; Endolysin Chain: A
Molecule details ›
Chain: A
Length: 501 amino acids
Theoretical weight: 56.72 KDa
Source organisms: Expression system: Spodoptera frugiperda
  • Canonical: P07550 (Residues: 1-230, 264-365; Coverage: 80%)
  • Canonical: P00720 (Residues: 2-162; Coverage: 98%)
Gene names: ADRB2, ADRB2R, B2AR, E
Sequence domains:
Structure domains: Rhodopsin 7-helix transmembrane proteins
Camelid Antibody Fragment Chain: B
Molecule details ›
Chain: B
Length: 126 amino acids
Theoretical weight: 13.78 KDa
Source organism: Lama glama
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 236.686Å b: 45.66Å c: 71.375Å
α: 90° β: 102.34° γ: 90°
R R work R free
0.243 0.235 0.308
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli