1l4d

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF MICROPLASMINOGEN-STREPTOKINASE ALPHA DOMAIN COMPLEX

Released:

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:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
PDBe Complex ID:
PDB-CPX-133231 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasmin light chain B Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00747 (Residues: 562-810; Coverage: 32%)
Gene name: PLG
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Streptokinase C Chain: B
Molecule details ›
Chain: B
Length: 122 amino acids
Theoretical weight: 13.46 KDa
Source organism: Streptococcus dysgalactiae subsp. equisimilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00779 (Residues: 40-173; Coverage: 30%)
Gene name: skc
Sequence domains: Staphylokinase/Streptokinase family
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 67.449Å b: 94.177Å c: 126.822Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.263
Expression system: Escherichia coli BL21