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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133233 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Angiostatin
Molecule details ›
Chains: A, X
Length: 234 amino acids
Theoretical weight: 26.76 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4
Length: 234 amino acids
Theoretical weight: 26.76 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
- Canonical:
P00747 (Residues: 100-333; Coverage: 30%)
Sequence domains: Kringle domain
Structure domains: Plasminogen Kringle 4
Plasminogen-binding group A streptococcal M-like protein PAM
Molecule details ›
Chains: B, C
Length: 30 amino acids
Theoretical weight: 3.64 KDa
Source organism: Streptococcus pyogenes
Expression system: Not provided
UniProt:
Sequence domains: Plasminogen (Pg) ligand in fibrinolytic pathway
Length: 30 amino acids
Theoretical weight: 3.64 KDa
Source organism: Streptococcus pyogenes
Expression system: Not provided
UniProt:
- Canonical: P49054 (Residues: 85-113; Coverage: 8%)
Sequence domains: Plasminogen (Pg) ligand in fibrinolytic pathway
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 5ID-B
Spacegroup:
P61
Expression systems:
- Komagataella pastoris
- Not provided
