› 2l0s

Solution NMR

Solution Structure of Human Plasminogen Kringle 3

Released:
DOI: 10.2210/pdb2l0s/pdb
PDB entry 2l0s coloured by chain, ensemble of 20 models, front view.
PDB entry 2l0s coloured by chain, ensemble of 20 models, side view.
PDB entry 2l0s coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape.
Christen MT, Frank P, Schaller J, Llinás M
Biochemistry 49 7131-50 (2010)
PMID: 20617841

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiostatin Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00747 (Residues: 272-354; 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
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Plasminogen receptors and their role in the pathogenesis of inflammatory, autoimmune and malignant disease.
Godier et al. (2013)
3 more

1 mention without citation

In Vitro Study of the Fibrinolytic Activity via Single Chain Urokinase-Type Plasminogen Activator and Molecular Docking of FGFC1.
Gao et al. (2021)