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Structure paper

TitleRole of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II.
Journal, issue, pagesBiochemistry, Vol. 47, Page 12028-12036, Year 2008
Publish dateJul 18, 2008 (structure data deposition date)
AuthorsZheng, J. / Avvaru, B.S. / Tu, C. / McKenna, R. / Silverman, D.N.
External linksBiochemistry / PubMed:18942852
MethodsX-ray diffraction
Resolution1.6 - 1.7 Å
Structure data

PDB-3dv7:
Role of Hydrophilic Residues in Proton Transfer During Catalysis by Human Carbonic Anhydrase II (N62A)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3dvb:
X-ray crystal structure of mutant N62V human Carbonic Anhydrase II
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3dvc:
X-ray crystal structure of mutant N62T of human Carbonic Anhydrase II
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3dvd:
X-ray crystal structure of mutant N62D of human Carbonic Anhydrase II
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLYASE / hCA II / Acetylation / Cytoplasm / Disease mutation / Metal-binding / Polymorphism / Zinc / Human carbonic anhydrase II / human carbonic anhydrase

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