› 8api

X-ray diffraction
3.1Å resolution

THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM

Released:
DOI: 10.2210/pdb8api/pdb
PDB entry 8api coloured by chain, front view.
PDB entry 8api coloured by chain, side view.
PDB entry 8api coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism.
Engh R, Löbermann H, Schneider M, Wiegand G, Huber R, Laurell CB
Protein Eng 2 407-15 (1989)
PMID: 2785270

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133785 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 347 amino acids
Theoretical weight: 39.11 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01009 (Residues: 36-382; Coverage: 88%)
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: 4.14 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01009 (Residues: 383-418; Coverage: 9%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand CYS 1 x CYS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6522
Unit cell:
a: 119.7Å b: 119.7Å c: 216.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 not available

Quick links

Citations

10 review citations

Natural protein proteinase inhibitors and their interaction with proteinases.
Bode et al. (1992)
9 more

1 mention without citation

Two physics-based models for pH-dependent calculations of protein solubility.
Spassov et al. (2022)