PDBe 1i5k

X-ray diffraction
2.7Å resolution

STRUCTURE AND BINDING DETERMINANTS OF THE RECOMBINANT KRINGLE-2 DOMAIN OF HUMAN PLASMINOGEN TO AN INTERNAL PEPTIDE FROM A GROUP A STREPTOCOCCAL SURFACE PROTEIN

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:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Angiostatin Chains: A, B
Molecule details ›
Chains: A, B
Length: 84 amino acids
Theoretical weight: 9.77 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: NEW P00747 (Residues: 184-264; Coverage: 10%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4
Plasminogen-binding group A streptococcal M-like protein PAM Chains: C, D
Molecule details ›
Chains: C, D
Length: 30 amino acids
Theoretical weight: 3.64 KDa
Source organism: Streptococcus pyogenes
Expression system: Not provided
UniProt:
  • Canonical: NEW P49054 (Residues: 85-114; Coverage: 8%)
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
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P6122
Unit cell:
a: 91.98Å b: 91.98Å c: 151.779Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.262
Expression systems:
  • Komagataella pastoris
  • Not provided