› 5zag

X-ray diffraction
1.95Å resolution

Function and Biology Details

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

Structure analysis Details

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

Ligands and Environments

1 bound ligand:
Ligand 94I 1 x 94I
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NFPSS BEAMLINE BL19U1
Spacegroup: R3
Unit cell:
a: 120.66Å b: 120.66Å c: 42.336Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.196 0.225
Expression system: Komagataella pastoris

Quick links

Citations

8 review citations

ENaC activation by proteases.
Anand et al. (2022)
7 more

1 mention without citation

6-Substituted Hexamethylene Amiloride (HMA) Derivatives as Potent and Selective Inhibitors of the Human Urokinase Plasminogen Activator for Use in Cancer.
Buckley et al. (2018)