PDBe 2doi

X-ray diffraction
3.1Å resolution

The X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcus protein PAM


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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Angiostatin Chains: A, X
Molecule details ›
Chains: A, X
Length: 234 amino acids
Theoretical weight: 26.76 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
  • Canonical: P00747 (Residues: 100-333; Coverage: 30%)
Gene name: PLG
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4
Plasminogen-binding group A streptococcal M-like protein PAM Chains: B, C
Molecule details ›
Chains: B, C
Length: 30 amino acids
Theoretical weight: 3.64 KDa
Source organism: Streptococcus pyogenes
Expression system: Not provided
  • Canonical: P49054 (Residues: 85-113; 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 5ID-B
Spacegroup: P61
Unit cell:
a: 58.467Å b: 58.467Å c: 389.146Å
α: 90° β: 90° γ: 120°
R R work R free
0.206 0.202 0.296
Expression systems:
  • Komagataella pastoris
  • Not provided