› 2znh

X-ray diffraction
2.8Å resolution

Crystal Structure of a Domain-Swapped Serpin Dimer

Released:
DOI: 10.2210/pdb2znh/pdb
PDB entry 2znh coloured by chain, front view.
PDB entry 2znh coloured by chain, side view.
PDB entry 2znh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization.
Yamasaki M, Li W, Johnson DJ, Huntington JA
Nature 455 1255-8 (2008)
PMID: 18923394

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Antithrombin-III Chains: A, B
Molecule details ›
Chains: A, B
Length: 432 amino acids
Theoretical weight: 49.1 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P01008 (Residues: 33-464; Coverage: 100%)
Gene names: AT3, PRO0309, SERPINC1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
2 bound ligands:
Ligand NAG 2 x NAG
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 71.35Å b: 99.88Å c: 92.46Å
α: 90° β: 100.62° γ: 90°
R-values:
R R work R free
0.201 0.201 0.247

Quick links

Citations

30 review citations

Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
Gooptu et al. (2009)
29 more

6 mentions without citation

Defining the mechanism of polymerization in the serpinopathies.
Ekeowa et al. (2010)
5 more