PDBe 1g37

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH-10556 AND EXOSITE-DIRECTED PEPTIDE

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin heavy chain Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 33.09 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 334-620; Coverage: 48%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
THROMBIN NONAPEPTIDE INHIBITOR Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.05 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 71.45Å b: 72.03Å c: 73.15Å
α: 90° β: 100.71° γ: 90°
R-values:
R R work R free
0.21 0.198 0.248
Expression system: Not provided