PDBe 3bei

X-ray diffraction
1.55Å resolution

Crystal structure of the slow form of thrombin in a self_inhibited conformation

Released:
Source organism: Homo sapiens
Primary publication:
Structural identification of the pathway of long-range communication in an allosteric enzyme.
Proc. Natl. Acad. Sci. U.S.A. 105 1832-7 (2008)
PMID: 18250335

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 Chain: A
Molecule details ›
Chain: A
Length: 44 amino acids
Theoretical weight: 5.15 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P00734 (Residues: 320-363; Coverage: 7%)
Gene name: F2
Structure domains: Thrombin light chain domain
Thrombin heavy chain Chain: B
Molecule details ›
Chain: B
Length: 259 amino acids
Theoretical weight: 29.78 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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P43
Unit cell:
a: 57.98Å b: 57.98Å c: 120.201Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.215
Expression system: Cricetulus griseus