PDBe 1eol

X-ray diffraction
2.1Å resolution

Design of P1' and P3' residues of trivalent thrombin inhibitors and their crystal structures

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: 289 amino acids
Theoretical weight: 33.21 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00734 (Residues: 332-620; Coverage: 48%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
THROMBIN INHIBITOR P628 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.91 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands

3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 71.1Å b: 71.9Å c: 73.3Å
α: 90° β: 100.5° γ: 90°
R-values:
R R work R free
0.193 0.193 0.24
Expression system: Not provided