The H163A mutation unravels an oxidized conformation of the SARS-CoV-2 main protease.

Tran N, Dasari S, Barwell SAE, McLeod MJ, Kalyaanamoorthy S, Holyoak T, Ganesan A, Nat Commun 14(1):5625 (2023) Europe PMC

SASDSQ5 – SARS-CoV-2 Main Protease H163A Mutant - 0.5 mg/mL

Replicase polyprotein 1ab, H3426A (3C-like proteinase nsp5 - H163A mutant)
MWexperimental 50 kDa
MWexpected 67 kDa
VPorod 74 nm3
log I(s) 8.43×10-3 8.43×10-4 8.43×10-5 8.43×10-6
Replicase polyprotein 1ab, H3426A (3C-like proteinase nsp5 - H163A mutant) small angle scattering data  s, nm-1
ln I(s)
Replicase polyprotein 1ab, H3426A (3C-like proteinase nsp5 - H163A mutant) Guinier plot ln 8.44×10-3 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Replicase polyprotein 1ab, H3426A (3C-like proteinase nsp5 - H163A mutant) Kratky plot 1.104 0 √3 sRg
p(r)
Replicase polyprotein 1ab, H3426A (3C-like proteinase nsp5 - H163A mutant) pair distance distribution function Rg: 2.6 nm 0 Dmax: 8.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of SARS-CoV-2 Main Protease (H163A) in 25 mM HEPES, 1 mM TCEP, pH 7.5 were collected on the ID7A1 BioSAXS / HP-Bio beam line at the Cornell High Energy Synchrotron Source (CHESS; Ithaca, NY, USA) using a Eiger 4M detector at a wavelength of λ = 0.11013 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.50 mg/ml was measured at 25°C. 15 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Sample detector distance = UNKNOWN

Replicase polyprotein 1ab, H3426A (3C-like proteinase nsp5 - H163A mutant) (MPro (H163A))
Mol. type   Protein
Organism   Severe acute respiratory syndrome coronavirus 2
Olig. state   Dimer
Mon. MW   33.7 kDa
 
UniProt   P0DTD1 (3264-3569)
Sequence   FASTA