› 3dru

X-ray diffraction
3.2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1-antitrypsin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 404 amino acids
Theoretical weight: 45.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 26-418; Coverage: 100%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 58.84Å b: 149.3Å c: 77.29Å
α: 90° β: 94.11° γ: 90°
R-values:
R R work R free
0.242 0.242 0.29
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The molecular and cellular pathology of α₁-antitrypsin deficiency.
Gooptu et al. (2014)
3 more

2 mentions without citation

Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha1-antitrypsin: implications for disease and drug design.
Gooptu et al. (2009)
1 more