› 5io1

X-ray diffraction
3.34Å resolution

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN Z ALPHA-1-ANTITRYPSIN

Released:
DOI: 10.2210/pdb5io1/pdb
PDB entry 5io1 coloured by chain, front view.
PDB entry 5io1 coloured by chain, side view.
PDB entry 5io1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular Mechanism of Z α1-Antitrypsin Deficiency.
Huang X, Zheng Y, Zhang F, Wei Z, Wang Y, Carrell RW, Read RJ, Chen GQ, Zhou A
J Biol Chem 291 15674-86 (2016)
PMID: 27246852

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 398 amino acids
Theoretical weight: 45.01 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P01009 (Residues: 29-418; Coverage: 99%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P21
Unit cell:
a: 74.138Å b: 53.675Å c: 110.144Å
α: 90° β: 96.88° γ: 90°
R-values:
R R work R free
0.218 0.215 0.275
Expression system: Drosophila melanogaster

Quick links

Citations

12 citation in other articles

The structural basis for Z α1-antitrypsin polymerization in the liver.
Faull et al. (2020)
11 more

4 mentions without citation

Alpha 1-Antitrypsin Deficiency: A Disorder of Proteostasis-Mediated Protein Folding and Trafficking Pathways.
Karatas et al. (2020)
3 more