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1DWK

STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE

Summary for 1DWK
Entry DOI10.2210/pdb1dwk/pdb
Related1DW9
DescriptorCYANATE HYDRATASE, SULFATE ION, OXALATE ION, ... (4 entities in total)
Functional Keywordslyase, cyanate degradation, psi, protein structure initiative, midwest center for structural genomics, mcsg
Biological sourceESCHERICHIA COLI
Total number of polymer chains10
Total formula weight175203.31
Authors
Walsh, M.A.,Otwinowski, Z.,Perrakis, A.,Anderson, P.M.,Joachimiak, A. (deposition date: 1999-12-07, release date: 2000-05-16, Last modification date: 2023-12-06)
Primary citationWalsh, M.A.,Otwinowski, Z.,Perrakis, A.,Anderson, P.M.,Joachimiak, A.
Structure of Cyanase Reveals that a Novel Dimeric and Decameric Arrangement of Subunits is Required for Formation of the Enzyme Active Site.
Structure, 8:505-, 2000
Cited by
PubMed: 10801492
DOI: 10.1016/S0969-2126(00)00134-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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