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7XID

S-ECD (Omicron) in complex with PD of ACE2

Summary for 7XID
Entry DOI10.2210/pdb7xid/pdb
EMDB information33203
DescriptorSpike glycoprotein, Angiotensin-converting enzyme 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordssars-cov-2, viral protein, viral protein-hydrolase complex, viral protein/hydrolase
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains5
Total formula weight630542.05
Authors
Li, Y.N.,Shen, Y.P.,Zhang, Y.Y.,Yan, R.H. (deposition date: 2022-04-12, release date: 2022-06-15, Last modification date: 2024-10-30)
Primary citationLi, Y.,Fan, Q.,Zhou, B.,Shen, Y.,Zhang, Y.,Cheng, L.,Qi, F.,Song, S.,Guo, Y.,Yan, R.,Ju, B.,Zhang, Z.
Structural and functional analysis of an inter-Spike bivalent neutralizing antibody against SARS-CoV-2 variants.
Iscience, 25:104431-104431, 2022
Cited by
PubMed Abstract: The different variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have attracted most public concern because they caused "wave and wave" COVID-19 pandemic. The initial step of viral infection is mediated by the SARS-CoV-2 Spike (S) protein, which mediates the receptor recognition and membrane fusion between virus and host cells. Neutralizing antibodies (nAbs) targeting the S protein of SARS-CoV-2 have become promising candidates for clinical intervention strategy, while multiple studies have shown that different variants have enhanced infectivity and antibody resistance. Here, we explore the structure and function of STS165, a broadly inter-Spike bivalent nAb against SARS-CoV-2 variants and even SARS-CoV, contributing to further understanding of the working mechanism of nAbs.
PubMed: 35607524
DOI: 10.1016/j.isci.2022.104431
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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