2pk4

X-ray diffraction
2.25Å resolution

THE REFINED STRUCTURE OF THE EPSILON-AMINOCAPROIC ACID COMPLEX OF HUMAN PLASMINOGEN KRINGLE

Released:

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: 80 amino acids
Theoretical weight: 9.17 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00747 (Residues: 375-454; 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: P21
Unit cell:
a: 42.21Å b: 35.46Å c: 25.43Å
α: 90° β: 102.94° γ: 90°
R-values:
R R work R free
0.148 not available not available
Expression system: Not provided