› 3cwl

X-ray diffraction
2.44Å resolution

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

Released:
DOI: 10.2210/pdb3cwl/pdb
PDB entry 3cwl coloured by chain, front view.
PDB entry 3cwl coloured by chain, side view.
PDB entry 3cwl 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

1 bound ligand:
Ligand CL 1 x CL
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P212121
Unit cell:
a: 39.225Å b: 51.898Å c: 206.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.264
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)
13 other articles

3 mentions without citation

Structural and functional characterization of a highly specific serpin in the insect innate immunity.
Park et al. (2011)
2 more