› 5ugg

X-ray diffraction
1.2Å resolution

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasmin light chain B Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 27.54 KDa
Source organism: Homo sapiens
Expression system: Komagataella phaffii GS115
UniProt:
  • Canonical: P00747 (Residues: 562-810; Coverage: 32%)
Gene name: PLG
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand 89M 1 x 89M
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P21
Unit cell:
a: 49.55Å b: 39.48Å c: 62.13Å
α: 90° β: 111.88° γ: 90°
R-values:
R R work R free
0.165 0.164 0.176
Expression system: Komagataella phaffii GS115

Quick links

Citations

3 review citations

Plant-Derived Compounds and Extracts as Modulators of Plasmin Activity-A Review.
Kolodziejczyk-Czepas et al. (2023)
2 more

3 mentions without citation

X-ray crystal structure of plasmin with tranexamic acid-derived active site inhibitors.
Law et al. (2017)
2 more