› 1dzg

X-ray diffraction
2.8Å resolution

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-133776 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Antithrombin-III Chain: I
Molecule details ›
Chain: I
Length: 432 amino acids
Theoretical weight: 49.13 KDa
Source organism: Homo sapiens
Expression system: Cricetinae gen. sp.
UniProt:
  • Canonical: P01008 (Residues: 33-464; Coverage: 100%)
Gene names: AT3, PRO0309, SERPINC1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Antithrombin-III Chain: L
Molecule details ›
Chain: L
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
2 bound ligands:
Ligand NAG 3 x NAG
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21
Unit cell:
a: 68.61Å b: 99.54Å c: 88.69Å
α: 90° β: 104.79° γ: 90°
R-values:
R R work R free
0.228 0.228 0.297
Expression system: Cricetinae gen. sp.

Quick links

Citations

11 review citations

Heparin-binding domains in vascular biology.
Muñoz et al. (2004)
10 more

1 mention without citation

Modeling of loops in proteins: a multi-method approach.
Jamroz et al. (2010)