› 2pf1

X-ray diffraction
2.8Å resolution

STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2pf1/pdb
PDB entry 2pf1 coloured by chain, front view.
PDB entry 2pf1 coloured by chain, side view.
PDB entry 2pf1 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structure of bovine prothrombin fragment 1 refined at 2.25 A resolution.
Seshadri TP, Tulinsky A, Skrzypczak-Jankun E, Park CH
J Mol Biol 220 481-94 (1991)
PMID: 1856869

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:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Activation peptide fragment 1 Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 18.02 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00735 (Residues: 44-199; Coverage: 26%)
Gene name: F2
Sequence domains:
Structure domains: Plasminogen Kringle 4

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CGU 10 x CGU

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 77.62Å b: 77.62Å c: 85.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

A player of many parts: the spotlight falls on thrombin's structure.
Stubbs et al. (1993)
4 more

2 mentions without citation

The linker connecting the two kringles plays a key role in prothrombin activation.
Pozzi et al. (2014)
1 more