5M77

a GH76 family enzyme structure

5M77 の概要

• エントリーDOI: 10.2210/pdb5m77/pdb
• 分子名称: Alpha-1,6-mannanase, 1-thio-alpha-D-mannopyranose-(1-6)-[(3S,4R,5R)-4,5-dihydroxypiperidin-3-yl]methyl 1-thio-alpha-D-mannopyranoside, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: glycoside hydrolase, complex, mannanase, s-linked polysaccharide, hydrolase
• 由来する生物種: Bacillus circulans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 133240.83

構造登録者

Jin, Y.,Williams, S.,Davies, G. (登録日: 2016-10-26, 公開日: 2017-08-09, 最終更新日: 2024-01-17)

主引用文献

Belz, T.,Jin, Y.,Coines, J.,Rovira, C.,Davies, G.J.,Williams, S.J.
An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor.
Chem. Commun. (Camb.), 53:9238-9241, 2017

PubMed Abstract: The non-hydrolyzable S-linked azasugars, 1,6-α-mannosylthio- and 1,6-α-mannobiosylthioisofagomine, were synthesized and shown to bind with high affinity to a family 76 endo-1,6-α-mannanase from Bacillus circulans. X-ray crystallography showed an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener.

PubMed: 28766587
DOI: 10.1039/c7cc04977c

実験手法

X-RAY DIFFRACTION (1.46 Å)