PDBe 2hpq

X-ray diffraction
3.3Å resolution

Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human ppack-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 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
UniProt:
  • 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
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Activation peptide fragment 2 Chain: P
Molecule details ›
Chain: P
Length: 79 amino acids
Theoretical weight: 8.69 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 213-291; Coverage: 13%)
Gene name: F2
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 123.6Å b: 123.6Å c: 101.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 not available not available