PDBe 1nrr

X-ray diffraction
2.4Å resolution

Crystallographic structures of Thrombin complexed with Thrombin receptor peptides: Existence of expected and novel binding modes


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 trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
Length: 259 amino acids
Theoretical weight: 29.78 KDa
Source organism: Homo sapiens
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Proteinase-activated receptor 1 Chain: R
Molecule details ›
Chain: R
Length: 18 amino acids
Theoretical weight: 2.34 KDa
Source organism: Homo sapiens
  • Canonical: P25116 (Residues: 43-60; Coverage: 5%)
Gene names: CF2R, F2R, PAR1, TR

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 71.3Å b: 72.2Å c: 72.3Å
α: 90° β: 100° γ: 90°
R R work R free
0.145 not available not available