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Structure paper

TitleStructural study of the uPA-nafamostat complex reveals a covalent inhibitory mechanism of nafamostat.
Journal, issue, pagesBiophys. J., Vol. 121, Page 3940-3949, Year 2022
Publish dateOct 7, 2021 (structure data deposition date)
AuthorsZhou, Y. / Wu, J. / Xue, G. / Li, J. / Jiang, L. / Huang, M.
External linksBiophys. J. / PubMed:36039386
MethodsX-ray diffraction
Resolution1.79 - 2.01 Å
Structure data

PDB-7vm4:
Crystal structure of uPA in complex with nafamostat
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-7vm5:
Crystal structure of uPA in complex with 4-guanidinobenzoic acid
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-7vm6:
Crystal structure of uPA in complex with 6-amidino-2-naphthol
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-7vm7:
Crystal structure of inactive uPA in complex with nafamostat
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-GBS:
4-carbamimidamidobenzoic acid / anticancer, anticoagulant, antivirus, protease inhibitor*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

ChemComp-7R8:
6-oxidanylnaphthalene-2-carboximidamide

ChemComp-SO4:
SULFATE ION

ChemComp-7RF:
(6-carbamimidoylnaphthalen-2-yl) 4-carbamimidamidobenzoate / anticancer, anticoagulant, antivirus, protease inhibitor*YM

Source
  • homo sapiens (human)
KeywordsHYDROLASE / uPA / serine protease / 4-guanidinobenzoic acid / 6-amidino-2-naphthol / nafamostat

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