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Structure paper

TitleConformational variability of different sulfonamide inhibitors with thienyl-acetamido moieties attributes to differential binding in the active site of cytosolic human carbonic anhydrase isoforms.
Journal, issue, pagesBioorg. Med. Chem., Vol. 19, Page 3732-3738, Year 2011
Publish dateMar 9, 2011 (structure data deposition date)
AuthorsBiswas, S. / Aggarwal, M. / Guzel, O. / Scozzafava, A. / McKenna, R. / Supuran, C.T.
External linksBioorg. Med. Chem. / PubMed:21620713
MethodsX-ray diffraction
Resolution1.6 - 1.7 Å
Structure data

PDB-3r16:
Human CAII bound to N-(4-sulfamoylphenyl)-2-(thiophen-2-yl) acetamide
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3r17:
hCarbonic anhydrase II bound to N-(2-fluoro.4-sulfamoylphenyl)-2-(thiophen-2-yl) acetamide
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-5UN:
N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HOH:
WATER

ChemComp-5UM:
N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide

Source
  • homo sapiens (human)
KeywordsLYASE / reversible hydration of carbondioxide

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