1avg

X-ray diffraction
2.6Å resolution

THROMBIN INHIBITOR FROM TRIATOMA PALLIDIPENNIS

Released:

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

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 41 amino acids
Theoretical weight: 4.79 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00735 (Residues: 326-366; Coverage: 7%)
Gene name: F2
Structure domains: Thrombin light chain domain
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
Length: 259 amino acids
Theoretical weight: 29.77 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00735 (Residues: 367-625; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Triabin Chain: I
Molecule details ›
Chain: I
Length: 142 amino acids
Theoretical weight: 16.04 KDa
Source organism: Meccus pallidipennis
Expression system: INSECT CELLS
UniProt:
  • Canonical: Q27049 (Residues: 19-160; Coverage: 100%)
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 44.84Å b: 67.23Å c: 183.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.275
Expression system: INSECT CELLS