› 1f92

X-ray diffraction
2.6Å resolution

Function and Biology Details

Reaction catalysed: 
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Urokinase-type plasminogen activator chain B Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 28.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00749 (Residues: 179-431; Coverage: 62%)
Gene name: PLAU
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand UKP 1 x UKP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 52.8Å b: 54.6Å c: 82.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.248
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Anti-tumour/metastasis effects of the potassium-sparing diuretic amiloride: an orally active anti-cancer drug waiting for its call-of-duty?
Matthews et al. (2011)
5 more

4 mentions without citation

Computational insights into binding of bisphosphates to farnesyl pyrophosphate synthase.
Ohno et al. (2011)
3 more