Function and Biology Details
Reaction catalysed:
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
Streptokinase C and Angiostatin (preferred)
PDBe Complex ID:
PDB-CPX-133231 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasmin light chain B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 27.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 250 amino acids
Theoretical weight: 27.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P00747 (Residues: 561-810; Coverage: 32%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Streptokinase C
Molecule details ›
Chains: C, D
Length: 362 amino acids
Theoretical weight: 41.16 KDa
Source organism: Streptococcus dysgalactiae subsp. equisimilis
UniProt:
Sequence domains: Staphylokinase/Streptokinase family
Structure domains:
Length: 362 amino acids
Theoretical weight: 41.16 KDa
Source organism: Streptococcus dysgalactiae subsp. equisimilis
UniProt:
- Canonical: P00779 (Residues: 38-399; Coverage: 87%)
Sequence domains: Staphylokinase/Streptokinase family
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P21
Expression system: Escherichia coli BL21
