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X-ray diffraction
1.91Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133787 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 404 amino acids
Theoretical weight: 45.61 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:
ACE-THR-THR-ALA-ILE-NH2 Chains: B, C
Molecule details ›
Chains: B, C
Length: 6 amino acids
Theoretical weight: 429 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2
Unit cell:
a: 113.71Å b: 38.96Å c: 93.13Å
α: 90° β: 100.13° γ: 90°
R-values:
R R work R free
0.192 0.19 0.225
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein.
Lechowicz et al. (2020)
1 more

1 mention without citation

An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.
Nyon et al. (2015)