X-ray diffraction
2.6Å resolution

Madanins (MEROPS I53) are cleaved by thrombin and factor Xa


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:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
Non-polymer only trimer (preferred)
Non-polymer only dimer
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin heavy chain Chains: A, H
Molecule details ›
Chains: A, 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
Thrombin light chain Chains: B, L
Molecule details ›
Chains: B, L
Length: 36 amino acids
Theoretical weight: 4.1 KDa
Source organism: Homo sapiens
  • Canonical: P00734 (Residues: 328-363; Coverage: 6%)
Gene name: F2
Inhibitor_I53 domain-containing protein Chain: M
Molecule details ›
Chain: M
Length: 60 amino acids
Theoretical weight: 6.78 KDa
Source organism: Haemaphysalis longicornis
Expression system: Escherichia coli
  • Canonical: Q86FP9 (Residues: 20-79; Coverage: 100%)

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 53.071Å b: 78.578Å c: 155.156Å
α: 90° β: 90° γ: 90°
R R work R free
0.193 0.191 0.239
Expression system: Escherichia coli