PDBe 3k65

X-ray diffraction
1.85Å resolution

Crystal Structure of Prethombin-2/Fragment-2 Complex

Source organism: Homo sapiens

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):
Activation peptide fragment 2 Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 12.62 KDa
Source organism: Homo sapiens
  • Canonical: P00734 (Residues: 199-314; Coverage: 19%)
Gene name: F2
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4
Thrombin heavy chain Chain: B
Molecule details ›
Chain: B
Length: 308 amino acids
Theoretical weight: 35.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P00734 (Residues: 315-622; Coverage: 52%)
Gene name: F2
Sequence domains:
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: DIAMOND BEAMLINE I04
Spacegroup: P41212
Unit cell:
a: 73.53Å b: 73.53Å c: 205.88Å
α: 90° β: 90° γ: 90°
R R work R free
0.221 0.213 0.229
Expression system: Escherichia coli