PDBe 1sgi

X-ray diffraction
2.3Å resolution

Crystal structure of the anticoagulant slow form of thrombin

Released:
Source organism: Homo sapiens
Primary publication:
Molecular dissection of Na+ binding to thrombin.
J. Biol. Chem. 279 31842-53 (2004)
PMID: 15152000

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin light chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Thrombin heavy chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 259 amino acids
Theoretical weight: 29.69 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P212121
Unit cell:
a: 61.85Å b: 68.07Å c: 162.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.251
Expression system: Cricetulus griseus