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Yorodumi- PDB-9cjp: X-ray crystal structure of SARS-CoV-2 main protease quadruple mut... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9cjp | |||||||||
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| Title | X-ray crystal structure of SARS-CoV-2 main protease quadruple mutants in complex with Nirmatrelvir | |||||||||
Components | 3C-like proteinase nsp5 | |||||||||
Keywords | HYDROLASE/INHIBITOR / HYDROLASE-INHIBITOR complex / SARS2 | |||||||||
| Function / homology | Function and homology informationprotein guanylyltransferase activity / RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Maturation of replicase proteins / TRAF3-dependent IRF activation pathway / ISG15-specific peptidase activity ...protein guanylyltransferase activity / RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism / mRNA guanylyltransferase activity / 5'-3' RNA helicase activity / Lyases; Phosphorus-oxygen lyases / Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / Maturation of replicase proteins / TRAF3-dependent IRF activation pathway / ISG15-specific peptidase activity / Transcription of SARS-CoV-2 sgRNAs / snRNP Assembly / Translation of Replicase and Assembly of the Replication Transcription Complex / Replication of the SARS-CoV-2 genome / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / double membrane vesicle viral factory outer membrane / SARS coronavirus main proteinase / host cell endoplasmic reticulum-Golgi intermediate compartment / 5'-3' DNA helicase activity / 3'-5'-RNA exonuclease activity / symbiont-mediated degradation of host mRNA / host cell endosome / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / symbiont-mediated suppression of host toll-like receptor signaling pathway / G-quadruplex RNA binding / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / omega peptidase activity / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / SARS-CoV-2 modulates host translation machinery / host cell Golgi apparatus / symbiont-mediated suppression of host NF-kappaB cascade / DNA helicase / symbiont-mediated perturbation of host ubiquitin-like protein modification / methyltransferase cap1 activity / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / single-stranded RNA binding / regulation of autophagy / lyase activity / viral protein processing / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / copper ion binding / symbiont-mediated suppression of host gene expression / symbiont-mediated activation of host autophagy / viral translational frameshifting / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / lipid binding / host cell nucleus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.71 Å | |||||||||
Authors | Esler, M.A. / Shi, K. / Harris, R.S. / Aihara, H. | |||||||||
| Funding support | United States, 2items
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Citation | Journal: Mbio / Year: 2025Title: Structural basis for varying drug resistance of SARS-CoV-2 M pro E166 variants. Authors: Esler, M.A. / Shi, K. / Rollie, J.A. / Delgado, R. / Vishwakarma, J. / Dabrowska, A. / Prahlad, J. / Moghadasi, S.A. / Harris, R.S. / Aihara, H. | |||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9cjp.cif.gz | 298 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9cjp.ent.gz | 200.9 KB | Display | PDB format |
| PDBx/mmJSON format | 9cjp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9cjp_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 9cjp_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 9cjp_validation.xml.gz | 27.3 KB | Display | |
| Data in CIF | 9cjp_validation.cif.gz | 35.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cj/9cjp ftp://data.pdbj.org/pub/pdb/validation_reports/cj/9cjp | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9cjoC ![]() 9cjqC ![]() 9cjrC ![]() 9cjsC ![]() 9cjtC ![]() 9cjuC ![]() 9cjvC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: ens_1
NCS oper: (Code: givenMatrix: (-0.999969553315, -0.00737532460864, -0.00254892731357), (-0.00779338208095, 0.960423825864, 0.27843372265), (0.000394511435814, 0.27844511003, -0.960452062865)Vector: ...NCS oper: (Code: given Matrix: (-0.999969553315, -0.00737532460864, -0.00254892731357), Vector: |
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Components
-Protein , 1 types, 2 molecules AB
| #1: Protein | Mass: 33825.633 Da / Num. of mol.: 2 / Mutation: T21I, L50F, S144A, E166V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rep, 1a-1b / Production host: ![]() References: UniProt: P0DTD1, SARS coronavirus main proteinase |
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-Non-polymers , 5 types, 101 molecules 








| #2: Chemical | | #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-SO4 / | #6: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.55 % |
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| Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop Details: J309: 0.1 M Buffer System 3, pH 8.5, 0.09M NPS, 50% v/v Precipitant Mix 4, MD Morpheus MD1-47 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.979 Å |
| Detector | Type: DECTRIS EIGER2 S 16M / Detector: PIXEL / Date: Mar 14, 2023 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
| Reflection | Resolution: 1.7→52.83 Å / Num. obs: 32792 / % possible obs: 91.5 % / Redundancy: 3 % / Biso Wilson estimate: 29.32 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.071 / Rpim(I) all: 0.047 / Rrim(I) all: 0.085 / Rsym value: 0.071 / Net I/σ(I): 6.1 |
| Reflection shell | Resolution: 1.7→1.93 Å / Rmerge(I) obs: 0.47 / Num. unique obs: 1640 / CC1/2: 0.785 / Rpim(I) all: 0.343 / Rrim(I) all: 0.585 / Rsym value: 0.47 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.71→52.83 Å / SU ML: 0.2276 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 30.6725 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 43.48 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 1.71→52.83 Å
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| Refine LS restraints |
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| Refine LS restraints NCS | Type: Torsion NCS / Rms dev position: 0.680872578618 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LS refinement shell |
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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X-RAY DIFFRACTION
United States, 2items
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