› 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:
DOI: 10.2210/pdb1cea/pdb
PDB entry 1cea coloured by chain, front view.
PDB entry 1cea coloured by chain, side view.
PDB entry 1cea coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the recombinant kringle 1 domain of human plasminogen in complexes with the ligands epsilon-aminocaproic acid and trans-4-(aminomethyl)cyclohexane-1-carboxylic Acid.
Mathews II, Vanderhoff-Hanaver P, Castellino FJ, Tulinsky A
Biochemistry 35 2567-76 (1996)
PMID: 8611560

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133230 (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: P00747 (Residues: 100-187; Coverage: 11%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:
Ligand ACA 2 x ACA
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

Quick links

Citations

8 review citations

Bacterial plasminogen activators and receptors.
Lähteenmäki et al. (2001)
7 more

7 mentions without citation

Amphibian-Derived Natural Anticancer Peptides and Proteins: Mechanism of Action, Application Strategies, and Prospects.
Chen et al. (2023)
6 more