› 2ant

X-ray diffraction
2.6Å resolution

THE 2.6 A STRUCTURE OF ANTITHROMBIN INDICATES A CONFORMATIONAL CHANGE AT THE HEPARIN BINDING SITE

Released:
DOI: 10.2210/pdb2ant/pdb
PDB entry 2ant coloured by chain, front view.
PDB entry 2ant coloured by chain, side view.
PDB entry 2ant coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site.
Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR
J Mol Biol 266 601-9 (1997)
PMID: 9067613

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:
1 distinct polypeptide molecule
Macromolecule:
Antithrombin-III Chains: I, L
Molecule details ›
Chains: I, 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P21
Unit cell:
a: 61.41Å b: 98.31Å c: 90.41Å
α: 90° β: 103.32° γ: 90°
R-values:
R R work R free
0.217 0.217 0.29

Quick links

Citations

11 review citations

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

11 mentions without citation

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