PDBe 1o5a

X-ray diffraction
1.68Å resolution

Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Urokinase-type plasminogen activator short chain A Chain: A
Molecule details ›
Chain: A
Length: 23 amino acids
Theoretical weight: 2.71 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: NEW P00749 (Residues: 156-178; Coverage: 6%)
Gene name: PLAU
Urokinase-type plasminogen activator chain B Chain: B
Molecule details ›
Chain: B
Length: 253 amino acids
Theoretical weight: 28.42 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: NEW P00749 (Residues: 179-431; Coverage: 62%)
Gene name: PLAU
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 81.78Å b: 49.87Å c: 66.74Å
α: 90° β: 113.41° γ: 90°
R-values:
R R work R free
0.212 0.209 0.245
Expression system: Komagataella pastoris