PDBe 4hfp

X-ray diffraction
2.4Å resolution

Structure of thrombin mutant S195a bound to the active site inhibitor argatroban

Released:
Source organism: Homo sapiens
Primary publication:
Autoactivation of thrombin precursors.
J. Biol. Chem. 288 11601-10 (2013)
PMID: 23467412

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thrombin light chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 31 amino acids
Theoretical weight: 3.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00734 (Residues: 333-363; Coverage: 5%)
Gene name: F2
Thrombin heavy chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 259 amino acids
Theoretical weight: 29.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00734 (Residues: 364-622; Coverage: 43%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P41
Unit cell:
a: 77.229Å b: 77.229Å c: 94.875Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.167 0.238
Expression system: Escherichia coli