7TW7

Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to SAM

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.62 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 

Starting Models: experimental
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This is version 1.3 of the entry. See complete history. 


Literature

High-resolution structures of the SARS-CoV-2 N7-methyltransferase inform therapeutic development.

Kottur, J., Rechkoblit, O., Quintana-Feliciano, R., Sciaky, D., Aggarwal, A.K.

(2022) Nat Struct Mol Biol 29: 850-853

  • DOI: https://doi.org/10.1038/s41594-022-00828-1
  • Primary Citation of Related Structures:  
    7TW7, 7TW8, 7TW9

  • PubMed Abstract: 

    Emergence of SARS-CoV-2 coronavirus has led to millions of deaths globally. We present three high-resolution crystal structures of the SARS-CoV-2 nsp14 N7-methyltransferase core bound to S-adenosylmethionine (1.62 Å), S-adenosylhomocysteine (1.55 Å) and sinefungin (1.41 Å). We identify features of the methyltransferase core that are crucial for the development of antivirals and show SAH as the best scaffold for the design of antivirals against SARS-CoV-2 and other pathogenic coronaviruses.

    • Organizational Affiliation: 

    Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. [email protected].


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription factor ETV6,Proofreading exoribonuclease nsp14 chimera309Severe acute respiratory syndrome coronavirus 2Mutation(s): 3 
Gene Names: ETV6, TEL, TEL1, rep, 1a-1b
EC: 3.1.13
UniProt & NIH Common Fund Data Resources
Find proteins for P41212 (Homo sapiens)
Explore P41212 
Go to UniProtKB:  P41212
PHAROS:  P41212
GTEx:  ENSG00000139083 
Find proteins for P0DTD1 (Severe acute respiratory syndrome coronavirus 2)
Explore P0DTD1 
Go to UniProtKB:  P0DTD1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP0DTD1P41212
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.62 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.181 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 108.774α = 90
b = 108.774β = 90
c = 48.527γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
DIALSdata reduction
Aimlessdata scaling
STARANISOdata scaling
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2022-09-07
    Type: Initial release
  • Version 1.1: 2022-09-21
    Changes: Database references
  • Version 1.2: 2022-10-05
    Changes: Database references
  • Version 1.3: 2023-10-18
    Changes: Data collection, Refinement description