› 2d26

X-ray diffraction
3.3Å resolution

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

Released:
DOI: 10.2210/pdb2d26/pdb
PDB entry 2d26 coloured by chain, front view.
PDB entry 2d26 coloured by chain, side view.
PDB entry 2d26 coloured by chain, top view.
Source organisms:
Primary publication:
Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase.
Dementiev A, Dobó J, Gettins PG
J Biol Chem 281 3452-7 (2006)
PMID: 16321984

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133452 (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
Sequence domains: Serpin (serine protease inhibitor)
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

Quick links

Citations

21 review citations

Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases.
Korkmaz et al. (2010)
20 more

22 mentions without citation

A Review of Alpha-1 Antitrypsin Binding Partners for Immune Regulation and Potential Therapeutic Application.
O'Brien et al. (2022)
21 more