PDBe 4h6t

X-ray diffraction
2.4Å resolution

Crystal structure of prethrombin-2 mutant E14eA/D14lA/E18A/S195A

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thrombin heavy chain Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 35.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00734 (Residues: 317-622; Coverage: 51%)
Gene name: F2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P41212
Unit cell:
a: 135.465Å b: 135.465Å c: 42.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.253
Expression system: Escherichia coli