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7C8D

Cryo-EM structure of cat ACE2 and SARS-CoV-2 RBD

7C8D の概要
エントリーDOI10.2210/pdb7c8d/pdb
EMDBエントリー30305
分子名称Angiotensin-converting enzyme 2, Spike protein S1, ZINC ION (3 entities in total)
機能のキーワードace2, sars-cov-2, cryo-em, complex, protein binding, hydrolase-viral protein complex, hydrolase/viral protein
由来する生物種Felis catus (Cat)
詳細
タンパク質・核酸の鎖数2
化学式量合計107071.86
構造登録者
Gao, G.F.,Wang, Q.H.,Wu, L.l. (登録日: 2020-05-29, 公開日: 2020-09-02, 最終更新日: 2025-06-25)
主引用文献Wu, L.,Chen, Q.,Liu, K.,Wang, J.,Han, P.,Zhang, Y.,Hu, Y.,Meng, Y.,Pan, X.,Qiao, C.,Tian, S.,Du, P.,Song, H.,Shi, W.,Qi, J.,Wang, H.W.,Yan, J.,Gao, G.F.,Wang, Q.
Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2.
Cell Discov, 6:68-68, 2020
Cited by
PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of the recent pandemic COVID-19, is reported to have originated from bats, with its intermediate host unknown to date. Here, we screened 26 animal counterparts of the human ACE2 (hACE2), the receptor for SARS-CoV-2 and SARS-CoV, and found that the ACE2s from various species, including pets, domestic animals and multiple wild animals, could bind to SARS-CoV-2 receptor binding domain (RBD) and facilitate the transduction of SARS-CoV-2 pseudovirus. Comparing to SARS-CoV-2, SARS-CoV seems to have a slightly wider range in choosing its receptor. We further resolved the cryo-electron microscopy (cryo-EM) structure of the cat ACE2 (cACE2) in complex with the SARS-CoV-2 RBD at a resolution of 3 Å, revealing similar binding mode as hACE2 to the SARS-CoV-2 RBD. These results shed light on pursuing the intermediate host of SARS-CoV-2 and highlight the necessity of monitoring susceptible hosts to prevent further outbreaks.
PubMed: 33020722
DOI: 10.1038/s41421-020-00210-9
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3 Å)
構造検証レポート
Validation report summary of 7c8d
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2026-03-04に公開中

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