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Solution NMR

SOLUTION STRUCTURE OF THE COMPLEX OF MUTANT VEK50[RH2/AA] AND PLASMINOGEN KRINGLE 2

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 analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-133233 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Angiostatin Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 10.17 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00747 (Residues: 179-262; Coverage: 11%)
Gene name: PLG
Sequence domains: Kringle domain
Plasminogen-binding group A streptococcal M-like protein PAM Chain: B
Molecule details ›
Chain: B
Length: 52 amino acids
Theoretical weight: 6.02 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: P49054 (Residues: 85-133; Coverage: 14%)
Gene names: emm, pam
Sequence domains: Plasminogen (Pg) ligand in fibrinolytic pathway

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression systems:
  • Komagataella pastoris
  • Escherichia coli