PDBe 1hag

X-ray diffraction
2Å resolution

THE ISOMORPHOUS STRUCTURES OF PRETHROMBIN2, HIRUGEN-AND PPACK-THROMBIN: CHANGES ACCOMPANYING ACTIVATION AND EXOSITE BINDING TO THROMBIN

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin heavy chain Chain: E
Molecule details ›
Chain: E
Length: 295 amino acids
Theoretical weight: 33.86 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00734 (Residues: 328-622; Coverage: 49%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hirudin-2' Chain: I
Molecule details ›
Chain: I
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P28505 (Residues: 55-64; Coverage: 15%)

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 72.85Å b: 71.32Å c: 72.63Å
α: 90° β: 101.1° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Not provided