X-ray diffraction
2.3Å resolution

Human alpha thrombin inhibited by RPPGF and hirugen

Source organism: Homo sapiens
Primary publication:
Mechanisms of Arg-Pro-Pro-Gly-Phe inhibition of thrombin.
Am. J. Physiol. Heart Circ. Physiol. 285 H183-93 (2003)
PMID: 12598231

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 tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Thrombin light chain Chain: 1
Molecule details ›
Chain: 1
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 Chain: 2
Molecule details ›
Chain: 2
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
Hirugen Chain: 3
Molecule details ›
Chain: 3
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Bradykinin Chain: 4
Molecule details ›
Chain: 4
Length: 5 amino acids
Theoretical weight: 574 Da
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P01042 (Residues: 381-385; Coverage: 1%)
Gene names: BDK, KNG, KNG1

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 79.15Å b: 104.97Å c: 45.18Å
α: 90° β: 90° γ: 90°
R R work R free
0.202 0.202 not available
Expression system: Not provided