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7C29

Esterase CrmE10 mutant-D178A

6M42」から置き換えられました6IQ8」から置き換えられました
7C29 の概要
エントリーDOI10.2210/pdb7c29/pdb
分子名称Carboxylesterase, 1,2-ETHANEDIOL, CALCIUM ION, ... (5 entities in total)
機能のキーワードesterase crme10 mutant-d178a, hydrolase
由来する生物種Croceicoccus marinus
タンパク質・核酸の鎖数2
化学式量合計45060.36
構造登録者
Li, Z.,Li, J. (登録日: 2020-05-07, 公開日: 2020-05-20, 最終更新日: 2023-11-29)
主引用文献Li, Z.,Li, L.,Huo, Y.,Chen, Z.,Zhao, Y.,Huang, J.,Jian, S.,Rong, Z.,Wu, D.,Gan, J.,Hu, X.,Li, J.,Xu, X.W.
Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases.
Biotechnol Biofuels, 13:107-107, 2020
Cited by
PubMed Abstract: Esterases and lipases hydrolyze short-chain esters and long-chain triglycerides, respectively, and therefore play essential roles in the synthesis and decomposition of ester bonds in the pharmaceutical and food industries. Many SGNH family esterases share high similarity in sequences. However, they have distinct enzymatic activities toward the same substrates. Due to a lack of structural information, the detailed catalytic mechanisms of these esterases remain barely investigated.
PubMed: 32549911
DOI: 10.1186/s13068-020-01742-8
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.18 Å)
構造検証レポート
Validation report summary of 7c29
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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