1DWK

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

1DWK の概要

• エントリーDOI: 10.2210/pdb1dwk/pdb
• 関連するPDBエントリー: 1DW9
• 分子名称: CYANATE HYDRATASE, SULFATE ION, OXALATE ION, ... (4 entities in total)
• 機能のキーワード: lyase, cyanate degradation, psi, protein structure initiative, midwest center for structural genomics, mcsg
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 175203.31

構造登録者

Walsh, M.A.,Otwinowski, Z.,Perrakis, A.,Anderson, P.M.,Joachimiak, A. (登録日: 1999-12-07, 公開日: 2000-05-16, 最終更新日: 2024-10-23)

主引用文献

Walsh, 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

PubMed Abstract: Cyanase is an enzyme found in bacteria and plants that catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. In Escherichia coli, cyanase is induced from the cyn operon in response to extracellular cyanate. The enzyme is functionally active as a homodecamer of 17 kDa subunits, and displays half-site binding of substrates or substrate analogs. The enzyme shows no significant amino acid sequence homology with other proteins.

PubMed: 10801492
DOI: 10.1016/S0969-2126(00)00134-9

実験手法

X-RAY DIFFRACTION (1.65 Å)