PDBe 1bml

X-ray diffraction
2.9Å resolution

COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Lys-|- > Arg-|-; higher selectivity than trypsin. Converts fibrin into soluble products.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasmin light chain B Chains: A, 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:
  • Canonical: P00747 (Residues: 561-810; Coverage: 32%)
Gene name: PLG
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Streptokinase C Chains: C, D
Molecule details ›
Chains: C, D
Length: 362 amino acids
Theoretical weight: 41.16 KDa
Source organism: Streptococcus dysgalactiae subsp. equisimilis
UniProt:
  • Canonical: P00779 (Residues: 38-399; Coverage: 87%)
Gene name: skc
Sequence domains: Staphylokinase/Streptokinase family
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 80.03Å b: 125.05Å c: 86.79Å
α: 90° β: 105.41° γ: 90°
R-values:
R R work R free
0.201 0.201 0.291
Expression system: Escherichia coli BL21