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2NSY

CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS IN COMPLEX WITH NAD-ADENYLATE

2NSY の概要
エントリーDOI10.2210/pdb2nsy/pdb
分子名称PROTEIN (NAD SYNTHETASE), MAGNESIUM ION, ADENOSINE MONOPHOSPHATE, ... (7 entities in total)
機能のキーワードligase, amidotransferase, nh3 dependent, atp pyrophosphatase
由来する生物種Bacillus subtilis
タンパク質・核酸の鎖数2
化学式量合計63262.61
構造登録者
Rizzi, M.,Bolognesi, M.,Coda, A. (登録日: 1998-07-14, 公開日: 1999-01-13, 最終更新日: 2023-08-30)
主引用文献Rizzi, M.,Bolognesi, M.,Coda, A.
A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure.
Structure, 6:1129-1140, 1998
Cited by
PubMed Abstract: Nicotinamide adenine dinucleotide (NAD+) has a central role in life processes. The ubiquitous enzyme NAD+ synthetase catalyzes a key step in NAD+ biosynthesis, transforming deamido-NAD+ into NAD+ by a two-step reaction. NAD+ synthetase belongs to the amidotransferase family and has been recognized as a member of the family of N-type ATP pyrophosphatases. In order to investigate the mechanism of the reaction carried out by NAD+ synthetase we have determined a high-resolution three-dimensional structure of the Bacillus subtilis homodimeric NAD+ synthetase in complex with the trapped reaction intermediate NAD-adenylate.
PubMed: 9753692
DOI: 10.1016/S0969-2126(98)00114-2
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2nsy
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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