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Yorodumi- PDB-9p6p: Crystal Structure of the SARS-CoV-2 2'-O-Methyltransferase with (... -
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Basic information
| Entry | Database: PDB / ID: 9p6p | ||||||
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| Title | Crystal Structure of the SARS-CoV-2 2'-O-Methyltransferase with (m7GpppA)pUpU (Cap-0) and S-Adenosyl-L-homocysteine (SAH). | ||||||
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Keywords | TRANSFERASE / Viral Protein / Center for Structural Biology of Infectious Diseases (CSBID) / 2'-O-Methyltransferase / Structural Genomics | ||||||
| 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 / host cell endoplasmic reticulum-Golgi intermediate compartment / double membrane vesicle viral factory outer membrane / SARS coronavirus main proteinase / 5'-3' DNA helicase activity / 3'-5'-RNA exonuclease activity / host cell endosome / symbiont-mediated degradation of host mRNA / mRNA guanylyltransferase / symbiont-mediated suppression of host ISG15-protein conjugation / G-quadruplex RNA binding / symbiont-mediated suppression of host toll-like receptor signaling pathway / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / omega peptidase activity / SARS-CoV-2 modulates host translation machinery / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / host cell Golgi apparatus / symbiont-mediated suppression of host NF-kappaB cascade / symbiont-mediated perturbation of host ubiquitin-like protein modification / DNA helicase / 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 / viral protein processing / host cell perinuclear region of cytoplasm / lyase activity / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host gene expression / copper ion binding / viral translational frameshifting / symbiont-mediated activation of host autophagy / 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: 1.95 Å | ||||||
Authors | Minasov, G. / Shuvalova, L. / Maltseva, N. / Kim, Y. / Kiryukhina, O. / Joachimiak, A. / Satchell, K.J.F. / Center for Structural Biology of Infectious Diseases (CSBID) | ||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Crystal Structure of the SARS-CoV-2 2'-O-Methyltransferase with (m7GpppA)pUpU (Cap-0) and S-Adenosyl-L-homocysteine (SAH). Authors: Minasov, G. / Shuvalova, L. / Maltseva, N. / Kim, Y. / Kiryukhina, O. / Joachimiak, A. / Satchell, K.J.F. / Center for Structural Biology of Infectious Diseases (CSBID) | ||||||
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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 | 9p6p.cif.gz | 370.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9p6p.ent.gz | 300.9 KB | Display | PDB format |
| PDBx/mmJSON format | 9p6p.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9p6p_validation.pdf.gz | 3.7 MB | Display | wwPDB validaton report |
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| Full document | 9p6p_full_validation.pdf.gz | 3.7 MB | Display | |
| Data in XML | 9p6p_validation.xml.gz | 45.5 KB | Display | |
| Data in CIF | 9p6p_validation.cif.gz | 62.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p6/9p6p ftp://data.pdbj.org/pub/pdb/validation_reports/p6/9p6p | HTTPS FTP |
-Related structure data
| Similar structure data | Similarity search - Function & homology F&H Search |
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| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-Protein , 2 types, 4 molecules ACBD
| #1: Protein | Mass: 33627.504 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rep, 1a-1b / Production host: ![]() References: UniProt: P0DTD1, Transferases; Transferring one-carbon groups; Methyltransferases #2: Protein | Mass: 15075.190 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: rep, 1a-1b / Plasmid: pMCSG53 / Production host: ![]() |
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-RNA chain , 1 types, 2 molecules EG
| #3: RNA chain | Mass: 1336.800 Da / Num. of mol.: 2 / Source method: obtained synthetically Source: (synth.) ![]() |
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-Non-polymers , 6 types, 564 molecules 










| #4: Chemical | | #5: Chemical | ChemComp-CL / #6: Chemical | ChemComp-SO4 / #7: Chemical | ChemComp-ZN / #8: Chemical | ChemComp-MGT / | #9: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 4.14 Å3/Da / Density % sol: 70.3 % |
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| Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: Protein: 3.8 mg/ml (nsp10/nsp16 1:1), 0.15M Sodium chloride, 0.01M Tris pH 7.5 , 2mM SAM, 1mM TCEP, 5% Glycerol; Screen: Classics II (B3), 0.5M Magnesium formate, 0.1M HEPES pH 7.5; Soak: 0. ...Details: Protein: 3.8 mg/ml (nsp10/nsp16 1:1), 0.15M Sodium chloride, 0.01M Tris pH 7.5 , 2mM SAM, 1mM TCEP, 5% Glycerol; Screen: Classics II (B3), 0.5M Magnesium formate, 0.1M HEPES pH 7.5; Soak: 0.5 hours, 0.2mM m7GpppAUU, 5mM SAH, in 2M Lithium sulfate. |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97913 Å |
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 29, 2021 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97913 Å / Relative weight: 1 |
| Reflection | Resolution: 1.95→30 Å / Num. obs: 117967 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 7.9 % / Biso Wilson estimate: 34 Å2 / CC1/2: 0.992 / CC star: 0.998 / Rmerge(I) obs: 0.167 / Rpim(I) all: 0.064 / Rsym value: 0.167 / Χ2: 1.006 / Net I/σ(I): 15.3 |
| Reflection shell | Resolution: 1.95→1.98 Å / Redundancy: 7.7 % / Mean I/σ(I) obs: 1.6 / Num. unique obs: 5809 / CC1/2: 0.43 / CC star: 0.776 / % possible all: 100 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.95→29.46 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.96 / SU B: 5.422 / SU ML: 0.08 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.102 / ESU R Free: 0.1 / Stereochemistry target values: MAXIMUM LIKELIHOODDetails: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 172.3 Å2 / Biso mean: 45.607 Å2 / Biso min: 23.44 Å2
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| Refinement step | Cycle: final / Resolution: 1.95→29.46 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 1.953→2.003 Å / Rfactor Rfree error: 0
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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X-RAY DIFFRACTION
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