› 1vr1

X-ray diffraction
1.9Å resolution

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133065 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thrombin light chain Chain: L
Molecule details ›
Chain: L
Length: 27 amino acids
Theoretical weight: 3.19 KDa
Source organism: Homo sapiens
Expression system: Cricetinae gen. sp.
UniProt:
  • Canonical: P00734 (Residues: 334-360; Coverage: 5%)
Gene name: F2
Sequence domains: Thrombin light chain
Thrombin heavy chain Chain: H
Molecule details ›
Chain: H
Length: 261 amino acids
Theoretical weight: 30.19 KDa
Source organism: Homo sapiens
Expression system: Cricetinae gen. sp.
UniProt:
  • Canonical: P00734 (Residues: 364-382, 383-388, 389-620; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Hirudin variant-1 Chain: I
Molecule details ›
Chain: I
Length: 10 amino acids
Theoretical weight: 1.36 KDa
Source organism: Hirudo medicinalis
Expression system: Cricetinae gen. sp.
UniProt:
  • Canonical: P01050 (Residues: 55-64; Coverage: 15%)

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TYS 1 x TYS

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 70.88Å b: 71.96Å c: 73.04Å
α: 90° β: 100.65° γ: 90°
R-values:
R R work R free
0.204 0.204 0.256
Expression system: Cricetinae gen. sp.

Quick links

Citations

3 review citations

Exosite determinants of serpin specificity.
Gettins et al. (2009)
2 more

2 mentions without citation

Side-chain flexibility in protein-ligand binding: the minimal rotation hypothesis.
Zavodszky et al. (2005)
1 more