X-ray diffraction
2.3Å resolution

Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism


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:
Non-polymer only 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
Salivary anti-thrombin peptide anophelin Chain: I
Molecule details ›
Chain: I
Length: 61 amino acids
Theoretical weight: 6.54 KDa
Source organism: Anopheles albimanus
Expression system: Escherichia coli
  • Canonical: Q9NJS1 (Residues: 23-83; Coverage: 100%)
Gene name: AT

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P3112
Unit cell:
a: 120.18Å b: 120.18Å c: 77.81Å
α: 90° β: 90° γ: 120°
R R work R free
0.171 0.169 0.201
Expression system: Escherichia coli