PDBe 5edk

X-ray diffraction
3.21Å resolution

Crystal structure of prothrombin deletion mutant residues 146-167 ( Form II ).

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prothrombin Chain: A
Molecule details ›
Chain: A
Length: 560 amino acids
Theoretical weight: 63.99 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P00734 (Residues: 44-622; Coverage: 93%)
Gene name: F2
Sequence domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P41212
Unit cell:
a: 84.192Å b: 84.192Å c: 346.427Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.293 0.291 0.323
Expression system: Mesocricetus auratus