PDBe 1h8i

X-ray diffraction
1.75Å resolution

X-ray crystal structure of human alpha-thrombin with a tripeptide phosphonate inhibitor.

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
Length: 253 amino acids
Theoretical weight: 29.21 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 42%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hirudin variant-1 Chain: I
Molecule details ›
Chain: I
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Source organism: Hirudo medicinalis
UniProt:
  • Canonical: P01050 (Residues: 55-64; Coverage: 15%)
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 27 amino acids
Theoretical weight: 3.19 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 334-360; Coverage: 5%)
Gene name: F2

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 70.393Å b: 71.301Å c: 72.416Å
α: 90° β: 100.87° γ: 90°
R-values:
R R work R free
0.186 0.186 0.235