PDBe 5edm

X-ray diffraction
2.2Å resolution

Crystal structure of prothrombin deletion mutant residues 154-167 ( Form I )

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: 568 amino acids
Theoretical weight: 64.84 KDa
Source organism: Homo sapiens
Expression system: Mesocricetus auratus
UniProt:
  • Canonical: P00734 (Residues: 44-622; Coverage: 95%)
Gene name: F2
Sequence domains:

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 109.884Å b: 168.69Å c: 144.315Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.236
Expression system: Mesocricetus auratus