› 2qug

X-ray diffraction
2Å resolution

Crystal structure of alpha-1-antitrypsin, crystal form A

Released:
DOI: 10.2210/pdb2qug/pdb
PDB entry 2qug coloured by chain, front view.
PDB entry 2qug coloured by chain, side view.
PDB entry 2qug coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Preventing serpin aggregation: the molecular mechanism of citrate action upon antitrypsin unfolding.
Pearce MC, Morton CJ, Feil SC, Hansen G, Adams JJ, Parker MW, Bottomley SP
Protein Sci 17 2127-33 (2008)
PMID: 18780818

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 Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 44.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 25-418; Coverage: 100%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 113.368Å b: 39.391Å c: 90.154Å
α: 90° β: 104.61° γ: 90°
R-values:
R R work R free
0.218 0.215 0.275
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.
Nyon et al. (2014)
11 other articles

8 mentions without citation

Preventing serpin aggregation: the molecular mechanism of citrate action upon antitrypsin unfolding.
Pearce et al. (2008)
7 more