PDBe 2d26

X-ray diffraction
3.3Å resolution

Active site distortion is sufficient for proteinase inhibit second crystal structure of covalent serpin-proteinase complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 40.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 25-382; Coverage: 91%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Structure domains:
Short peptide from AAT Chain: B
Molecule details ›
Chain: B
Length: 36 amino acids
Theoretical weight: 4.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 383-418; Coverage: 9%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Chymotrypsin-like elastase family member 1 Chain: C
Molecule details ›
Chain: C
Length: 240 amino acids
Theoretical weight: 25.93 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00772 (Residues: 27-266; Coverage: 96%)
Gene names: CELA1, ELA1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 109.83Å b: 85.18Å c: 76.26Å
α: 90° β: 121.01° γ: 90°
R-values:
R R work R free
0.274 0.251 0.312
Expression system: Escherichia coli