Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5H9Y

Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose.

5H9Y の概要
エントリーDOI10.2210/pdb5h9y/pdb
関連するPDBエントリー5H9X
分子名称beta-1,3-glucanase, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, ... (5 entities in total)
機能のキーワードbeta-1, 3-glucan recognition, glycoside hydrolase family 64, 3-glucanase, gh64-tlp-sf superfamily, hydrolase
由来する生物種Paenibacillus barengoltzii
タンパク質・核酸の鎖数1
化学式量合計50663.20
構造登録者
Zhen, Q.,Yan, Q.,Yang, S.,Jiang, Z.,You, X. (登録日: 2015-12-29, 公開日: 2017-02-15, 最終更新日: 2023-11-08)
主引用文献Qin, Z.,Yang, D.,You, X.,Liu, Y.,Hu, S.,Yan, Q.,Yang, S.,Jiang, Z.
The recognition mechanism of triple-helical beta-1,3-glucan by a beta-1,3-glucanase
Chem. Commun. (Camb.), 53:9368-9371, 2017
Cited by
PubMed Abstract: β-1,3-Glucan is one of the most abundant polysaccharides in fungi. Recognition of β-1,3-glucan occurs in both hydrolysis by glycoside hydrolases and immunological recognition. Our study provides a novel structural account of how glycoside hydrolase recognizes and hydrolyzes substrates in a triple-helical form and presents a general structural basis of β-1,3-glucan recognition.
PubMed: 28787048
DOI: 10.1039/c7cc03330c
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.969 Å)
構造検証レポート
Validation report summary of 5h9y
検証レポート(詳細版)ダウンロードをダウンロード

227111

件を2024-11-06に公開中

PDB statisticsPDBj update infoContact PDBjnumon