Zinc in PDB 7wri: Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2

Enzymatic activity of Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2

All present enzymatic activity of Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2:
3.4.17.23;

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2 (pdb code 7wri). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2, PDB code: 7wri:

Zinc binding site 1 out of 1 in 7wri

Go back to Zinc Binding Sites List in 7wri
Zinc binding site 1 out of 1 in the Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Sars-Cov-2 Omicron Spike Receptor-Binding Domain in Complex with Mouse ACE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:53.9
occ:1.00
NE2 A:HIS374 2.1 26.1 1.0
OE2 A:GLU402 2.1 22.0 1.0
NE2 A:HIS378 2.1 23.9 1.0
CE1 A:HIS378 2.9 23.9 1.0
CD2 A:HIS374 3.0 26.1 1.0
CE1 A:HIS374 3.0 26.1 1.0
CD A:GLU402 3.1 22.0 1.0
CD2 A:HIS378 3.1 23.9 1.0
OE1 A:GLU402 3.6 22.0 1.0
ND1 A:HIS374 4.0 26.1 1.0
ND1 A:HIS378 4.0 23.9 1.0
CG A:HIS374 4.0 26.1 1.0
CG A:HIS378 4.1 23.9 1.0
CG A:GLU402 4.3 22.0 1.0
OE2 A:GLU375 4.4 27.8 1.0
O A:HIS374 4.6 26.1 1.0

Reference:

L.Li, P.Han, B.Huang, Y.Xie, W.Li, D.Zhang, P.Han, Z.Xu, B.Bai, J.Zhou, X.Kang, X.Li, A.Zheng, R.Zhang, S.Qiao, X.Zhao, J.Qi, Q.Wang, K.Liu, G.F.Gao. Broader-Species Receptor Binding and Structural Bases of Omicron Sars-Cov-2 to Both Mouse and Palm-Civet ACE2S. Cell Discov V. 8 65 2022.
ISSN: ESSN 2056-5968
PubMed: 35821014
DOI: 10.1038/S41421-022-00431-0
Page generated: Sat Apr 8 05:20:51 2023

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