3O82

Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl] adenosine

3O82 の概要

• エントリーDOI: 10.2210/pdb3o82/pdb
• 関連するPDBエントリー: 3O83 3O84
• 分子名称: Peptide arylation enzyme, 5'-O-{[(2,3-dihydroxyphenyl)carbonyl]sulfamoyl}adenosine, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: ligase, adenylation of 2, 3-dihydroxybenzoate and transfer to pantetheine cofactor of basf, non-ribosomal peptide synthetase (nrps)
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122861.70

構造登録者

Drake, E.J.,Duckworth, B.P.,Neres, J.,Aldrich, C.C.,Gulick, A.M. (登録日: 2010-08-02, 公開日: 2010-10-06, 最終更新日: 2023-09-06)

• 主引用文献: Drake, E.J.,Duckworth, B.P.,Neres, J.,Aldrich, C.C.,Gulick, A.M.; Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.; Biochemistry, 49:9292-9305, 2010; PubMed: 20853905; DOI: 10.1021/bi101226n

実験手法

X-RAY DIFFRACTION (2.7 Å)