5YNQ

Crystal structure of MERS-CoV nsp16/nsp10 complex bound to SAH and m7GpppG

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history. 


Literature

Structural insights into the molecular mechanism of MERS Coronavirus RNA ribose 2'-O-methylation by nsp16/nsp10 protein complex

Wei, S.M., Yang, L., Ke, Z.H., Liu, Q.Y., Yang, Z.Z., Chen, Y., Guo, D.Y., Fan, C.P.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
nsp16 protein303Human betacoronavirus 2c EMC/2012Mutation(s): 0 
Gene Names: orf1ab
UniProt
Find proteins for K0BWD0 (Human betacoronavirus 2c EMC/2012)
Explore K0BWD0 
Go to UniProtKB:  K0BWD0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupK0BWD0
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
nsp10 protein140Human betacoronavirus 2c EMC/2012Mutation(s): 0 
Gene Names: orf1ab
UniProt
Find proteins for K4LC41 (Human betacoronavirus 2c EMC/2012)
Explore K4LC41 
Go to UniProtKB:  K4LC41
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupK4LC41
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 
  • Space Group: P 21 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.874α = 90
b = 70.101β = 90
c = 118.937γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
NSFCChina31570762

Revision History  (Full details and data files)

  • Version 1.0: 2018-12-05
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Refinement description