PDBe 3hat

X-ray diffraction
2.5Å resolution

ACTIVE SITE MIMETIC INHIBITION OF THROMBIN

Released:
Source organisms:
Primary publication:
Active-site mimetic inhibition of thrombin.
Acta Crystallogr. D Biol. Crystallogr. 51 550-9 (1995)
PMID: 15299843

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 tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 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
Hirudin variant-2 Chain: I
Molecule details ›
Chain: I
Length: 12 amino acids
Theoretical weight: 1.53 KDa
Source organism: Hirudo medicinalis
Expression system: Not provided
UniProt:
  • Canonical: P09945 (Residues: 60-71; Coverage: 19%)
FPAM (FIBRINOPEPTIDE A MIMIC) Chain: T
Molecule details ›
Chain: T
Length: 6 amino acids
Theoretical weight: 701 Da

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 71.1Å b: 72.4Å c: 73Å
α: 90° β: 101° γ: 90°
R-values:
R R work R free
0.14 not available not available
Expression system: Not provided