X-ray diffraction
2.56Å resolution

X-ray structure of the complex between human thrombin and the TBA deletion mutant lacking thymine 3 nucleobase


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:
2 distinct polypeptide molecules
1 distinct DNA molecule
Macromolecules (3 distinct):
Thrombin light chain Chains: A, C
Molecule details ›
Chains: A, C
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 Chains: B, D
Molecule details ›
Chains: B, D
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 Binding Aptamer (TBA) Chains: E, F
Molecule details ›
Chains: E, F
Length: 15 nucleotides
Theoretical weight: 4.62 KDa

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 61.736Å b: 120.725Å c: 67.233Å
α: 90° β: 94.22° γ: 90°
R R work R free
0.171 0.168 0.227