1pkr

X-ray diffraction
2.48Å resolution

THE STRUCTURE OF RECOMBINANT PLASMINOGEN KRINGLE 1 AND THE FIBRIN BINDING SITE

Released:
Source organism: Homo sapiens
Primary publication:
The structure of recombinant plasminogen kringle 1 and the fibrin binding site.
Blood Coagul. Fibrinolysis 5 157-66 (1994)
PMID: 8054447

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiostatin Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.41 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00747 (Residues: 101-182; Coverage: 10%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 58.93Å b: 58.93Å c: 54.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 not available not available
Expression system: Not provided