PDBe 5hpg

X-ray diffraction
1.66Å resolution

STRUCTURE AND LIGAND DETERMINANTS OF THE RECOMBINANT KRINGLE 5 DOMAIN OF HUMAN PLASMINOGEN

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmin heavy chain A, short form Chains: A, B
Molecule details ›
Chains: A, B
Length: 84 amino acids
Theoretical weight: 9.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P00747 (Residues: 480-563; Coverage: 11%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 77.43Å b: 79.2Å c: 30.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.166 not available
Expression system: Escherichia coli