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TitleEngineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.
Journal, issue, pagesBiochemistry, Vol. 37, Page 3297-3304, Year 1998
Publish dateAug 12, 1997 (structure data deposition date)
AuthorsLukacs, C.M. / Rubin, H. / Christianson, D.W.
External linksBiochemistry / PubMed:9521649
MethodsX-ray diffraction
Resolution2.1 - 2.9 Å
Structure data

PDB-1as4:
CLEAVED ANTICHYMOTRYPSIN A349R
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3caa:
CLEAVED ANTICHYMOTRYPSIN A347R
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4caa:
CLEAVED ANTICHYMOTRYPSIN T345R
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSERPIN / SERINE PROTEASE INHIBITOR / ANTICHYMOTRYPSIN

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