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Yorodumi- PDB-7u28: Structure of SARS-CoV-2 Mpro Lambda (G15S) in complex with Nirmat... -
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-Basic information
Entry | Database: PDB / ID: 7u28 | ||||||
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Title | Structure of SARS-CoV-2 Mpro Lambda (G15S) in complex with Nirmatrelvir (PF-07321332) | ||||||
Components | 3C-like proteinase nsp5 | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / Protease / SARS-CoV-2 / covalent complex / inhibitor / HYDROLASE-INHIBITOR complex / Omicron / PF-07321332 / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information viral genome replication / methyltransferase activity / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-2 genome / methylation / double membrane vesicle viral factory outer membrane ...viral genome replication / methyltransferase activity / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / Maturation of replicase proteins / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-2 genome / methylation / double membrane vesicle viral factory outer membrane / SARS coronavirus main proteinase / host cell endosome / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / SARS-CoV-2 modulates host translation machinery / omega peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / host cell Golgi apparatus / symbiont-mediated perturbation of host ubiquitin-like protein modification / endonuclease activity / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / viral protein processing / induction by virus of host autophagy / symbiont-mediated suppression of host gene expression / cysteine-type endopeptidase activity / lipid binding / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / SARS-CoV-2 activates/modulates innate and adaptive immune responses / proteolysis / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | Severe acute respiratory syndrome coronavirus 2 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.679 Å | ||||||
Authors | Greasley, S.E. / Ferre, R.A. / Plotnikova, O. / Liu, W. / Stewart, A.E. | ||||||
Funding support | 1items
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Citation | Journal: J.Biol.Chem. / Year: 2022 Title: Structural basis for the in vitro efficacy of nirmatrelvir against SARS-CoV-2 variants. Authors: Greasley, S.E. / Noell, S. / Plotnikova, O. / Ferre, R. / Liu, W. / Bolanos, B. / Fennell, K. / Nicki, J. / Craig, T. / Zhu, Y. / Stewart, A.E. / Steppan, C.M. #1: Journal: Biorxiv / Year: 2022 Title: Structural basis for Nirmatrelvir in vitro efficacy against the Omicron variant of SARS-CoV-2 Authors: Greasley, S.E. / Noell, S. / Plotnikova, O. / Ferre, R. / Liu, W. / Bolanos, B. / Fennell, K. / Nicki, J. / Craig, T. / Zhu, Y. / Stewart, A.E. / Steppan, C.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7u28.cif.gz | 130.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7u28.ent.gz | 106.7 KB | Display | PDB format |
PDBx/mmJSON format | 7u28.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u2/7u28 ftp://data.pdbj.org/pub/pdb/validation_reports/u2/7u28 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 33855.570 Da / Num. of mol.: 2 / Mutation: G15S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Severe acute respiratory syndrome coronavirus 2 Production host: Escherichia coli (E. coli) References: UniProt: P0DTC1, SARS coronavirus main proteinase #2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.48 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop Details: 24.0 %w/v PEG 3350 and 0.2 M sodium sulfate decahydrate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å |
Detector | Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Feb 6, 2022 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.68→112.33 Å / Num. obs: 46261 / % possible obs: 74.2 % / Redundancy: 3.4 % / CC1/2: 0.998 / Rmerge(I) obs: 0.064 / Rpim(I) all: 0.041 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 1.68→1.78 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.595 / Num. unique obs: 2314 / CC1/2: 0.601 / Rpim(I) all: 0.454 / % possible all: 46.4 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 1.679→112.33 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.935 / SU R Cruickshank DPI: 0.17 / Cross valid method: THROUGHOUT / SU R Blow DPI: 0.171 / SU Rfree Blow DPI: 0.151 / SU Rfree Cruickshank DPI: 0.151
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Displacement parameters | Biso mean: 23.93 Å2
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.679→112.33 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.68→1.74 Å
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