PDBe 1cea

X-ray diffraction
2.06Å resolution

THE STRUCTURE OF THE NON-COVALENT COMPLEX OF RECOMBINANT KRINGLE 1 DOMAIN OF HUMAN PLASMINOGEN WITH EACA (EPSILON-AMINOCAPROIC ACID)

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiostatin Chains: A, B
Molecule details ›
Chains: A, B
Length: 88 amino acids
Theoretical weight: 10.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P00747 (Residues: 100-187; Coverage: 11%)
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
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 34.5Å b: 51.6Å c: 46.5Å
α: 90° β: 112° γ: 90°
R-values:
R R work R free
0.168 not available not available
Expression system: Escherichia coli