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:
- Serine proteases, trypsin domain
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
- Peptidase S1, PA clan, chymotrypsin-like fold
- Peptidase S1, PA clan
- Staphylokinase
- Staphylokinase/Streptokinase superfamily
Structure domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Staphylokinase and Angiostatin (preferred)
PDBe Complex ID:
PDB-CPX-133238 (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: 27.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 250 amino acids
Theoretical weight: 27.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P00747 (Residues: 561-810; Coverage: 32%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Staphylokinase
Molecule details ›
Chain: C
Length: 128 amino acids
Theoretical weight: 14.6 KDa
Source organism: Staphylococcus phage 42D.m
UniProt:
Sequence domains: Staphylokinase/Streptokinase family
Structure domains: Ubiquitin-like (UB roll)
Length: 128 amino acids
Theoretical weight: 14.6 KDa
Source organism: Staphylococcus phage 42D.m
UniProt:
- Canonical: P15240 (Residues: 38-163; Coverage: 93%)
Sequence domains: Staphylokinase/Streptokinase family
Structure domains: Ubiquitin-like (UB roll)
