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Structure paper

TitleCrystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions.
Journal, issue, pagesEur. J. Biochem., Vol. 210, Page 867-871, Year 1992
Publish dateJul 2, 1992 (structure data deposition date)
AuthorsMangani, S. / Hakansson, K.
External linksEur. J. Biochem. / PubMed:1336460
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1can:
CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1cao:
CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HG:
Unknown entry

ChemComp-NO3:
NITRATE ION

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-H2S:
HYDROSULFURIC ACID

Source
  • homo sapiens (human)
KeywordsLYASE(OXO-ACID)

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