3MLA

BaNadD in complex with inhibitor 1_02

3MLA の概要

• エントリーDOI: 10.2210/pdb3mla/pdb
• 関連するPDBエントリー: 3MLB 3MMX
• 分子名称: nicotinate-nucleotide adenylyltransferase, 4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: nmnat-inhibitor complex, transferase
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45037.19

構造登録者

Huang, N.,Eyobo, Y.,Zhang, H. (登録日: 2010-04-16, 公開日: 2010-07-28, 最終更新日: 2023-09-06)

主引用文献

Huang, N.,Kolhatkar, R.,Eyobo, Y.,Sorci, L.,Rodionova, I.,Osterman, A.L.,Mackerell, A.D.,Zhang, H.
Complexes of bacterial nicotinate mononucleotide adenylyltransferase with inhibitors: implication for structure-based drug design and improvement.
J.Med.Chem., 53:5229-5239, 2010

PubMed Abstract: Bacterial nicotinate mononucleotide adenylyltransferase encoded by the essential gene nadD plays a central role in the synthesis of the redox cofactor NAD(+). The NadD enzyme is conserved in the majority of bacterial species and has been recognized as a novel target for developing new and potentially broad-spectrum antibacterial therapeutics. Here we report the crystal structures of Bacillus anthracis NadD in complex with three NadD inhibitors, including two analogues synthesized in the present study. These structures revealed a common binding site shared by different classes of NadD inhibitors and explored the chemical environment surrounding this site. The structural data obtained here also showed that the subtle changes in ligand structure can lead to significant changes in the binding mode, information that will be useful for future structure-based optimization and design of high affinity inhibitors.

PubMed: 20578699
DOI: 10.1021/jm100377f

実験手法

X-RAY DIFFRACTION (1.75 Å)