PDBe 1d5s

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURE OF CLEAVED ANTITRYPSIN POLYMER

Released:
Source organism: Homo sapiens

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 37.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 44-377; Coverage: 85%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Structure domains:
Short peptide from AAT Chain: B
Molecule details ›
Chain: B
Length: 41 amino acids
Theoretical weight: 4.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 378-418; Coverage: 10%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Structure domains: Serpins superfamily

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P42212
Unit cell:
a: 110.17Å b: 110.17Å c: 76.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.262
Expression system: Escherichia coli