PDBe 1gi8

X-ray diffraction
1.75Å resolution

A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE

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: 245 amino acids
Theoretical weight: 27.58 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: NEW P00749 (Residues: 179-423; Coverage: 60%)
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 RU200
Spacegroup: C2
Unit cell:
a: 82.2Å b: 48.77Å c: 67.02Å
α: 90° β: 113.53° γ: 90°
R-values:
R R work R free
0.204 0.2 0.254
Expression system: Komagataella pastoris