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TitleStructure of Cyanase Reveals that a Novel Dimeric and Decameric Arrangement of Subunits is Required for Formation of the Enzyme Active Site
Journal, issue, pagesStructure, Vol. 8, Page 505-, Year 2000
Publish dateDec 3, 1999 (structure data deposition date)
AuthorsWalsh, M.A. / Otwinowski, Z. / Perrakis, A. / Anderson, P.M. / Joachimiak, A.
External linksStructure / PubMed:10801492
MethodsX-ray diffraction
Resolution1.65 Å
Structure data

PDB-1dw9:
Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-1dwk:
STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-OXL:
OXALATE ION

Source
  • escherichia coli (E. coli)
KeywordsLYASE / CYANATE DEGRADATION / STRUCTURAL GENOMICS / PSI / PROTEIN STRUCTURE INITIATIVE / MIDWEST CENTER FOR STRUCTURAL GENOMICS / MCSG

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