› 1qmn

X-ray diffraction
2.27Å resolution

Alpha1-antichymotrypsin serpin in the delta conformation (partial loop insertion)

Released:
DOI: 10.2210/pdb1qmn/pdb
PDB entry 1qmn coloured by chain, front view.
PDB entry 1qmn coloured by chain, side view.
PDB entry 1qmn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease.
Gooptu B, Hazes B, Chang WS, Dafforn TR, Carrell RW, Read RJ, Lomas DA
Proc Natl Acad Sci U S A 97 67-72 (2000)
PMID: 10618372

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1-antichymotrypsin Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 45.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01011 (Residues: 26-423; Coverage: 100%)
Gene names: AACT, GIG24, GIG25, SERPINA3
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P21
Unit cell:
a: 41.723Å b: 122.094Å c: 41.724Å
α: 90° β: 101.03° γ: 90°
R-values:
R R work R free
0.197 0.197 0.243
Expression system: Escherichia coli

Quick links

Citations

27 review citations

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

11 mentions without citation

An overview of the serpin superfamily.
Law et al. (2006)
10 more