STRUCTURE OF CYANASE REVEALS THAT A NOVEL DIMERIC AND DECAMERIC ARRANGEMENT OF SUBUNITS IS REQUIRED FOR FORMATION OF THE ENZYME ACTIVE SITE
The structure was published by Walsh, M.A., Otwinowski, Z., Perrakis, A., Anderson, P.M., and Joachimiak, A., in 2000 in a paper entitled "Structure of Cyanase Reveals that a Novel Dimeric and Decameric Arrangement of Subunits is Required for Formation of the Enzyme Active Site" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.65 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of CYANATE LYASE.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homodecamers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: