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Yorodumi- PDB-7nxc: Crystal structure of the receptor binding domain of SARS-CoV-2 P.... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 7nxc | |||||||||
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| Title | Crystal structure of the receptor binding domain of SARS-CoV-2 P.1 variant Spike glycoprotein in complex with ACE2 | |||||||||
Components |
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Keywords | VIRAL PROTEIN/HYDROLASE / SARS-CoV-2 B.1.1.7 variant / B.1.351 variant / P.1 variant / antibody / receptor-binding-domain / spike / neutralisation / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN / HYDROLASE / VIRAL PROTEIN-HYDROLASE complex | |||||||||
| Function / homology | Function and homology informationpositive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / positive regulation of gap junction assembly / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / regulation of cardiac conduction / maternal process involved in female pregnancy ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / positive regulation of gap junction assembly / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / regulation of cardiac conduction / maternal process involved in female pregnancy / peptidyl-dipeptidase activity / regulation of vasoconstriction / transporter activator activity / Metabolism of Angiotensinogen to Angiotensins / carboxypeptidase activity / angiotensin maturation / viral life cycle / Attachment and Entry / receptor-mediated endocytosis of virus by host cell / metallocarboxypeptidase activity / positive regulation of cardiac muscle contraction / regulation of cytokine production / blood vessel diameter maintenance / negative regulation of smooth muscle cell proliferation / brush border membrane / negative regulation of ERK1 and ERK2 cascade / positive regulation of reactive oxygen species metabolic process / metallopeptidase activity / endocytic vesicle membrane / regulation of cell population proliferation / virus receptor activity / regulation of inflammatory response / symbiont-mediated disruption of host tissue / endopeptidase activity / Maturation of spike protein / Translation of Structural Proteins / Virion Assembly and Release / host cell surface / viral translation / host extracellular space / symbiont-mediated-mediated suppression of host tetherin activity / Induction of Cell-Cell Fusion / Potential therapeutics for SARS / structural constituent of virion / membrane fusion / entry receptor-mediated virion attachment to host cell / Attachment and Entry / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of viral entry into host cell / receptor-mediated virion attachment to host cell / host cell surface receptor binding / cilium / symbiont-mediated suppression of host innate immune response / apical plasma membrane / receptor ligand activity / membrane raft / endocytosis involved in viral entry into host cell / endoplasmic reticulum lumen / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / symbiont entry into host cell / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / virion membrane / cell surface / negative regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / extracellular region / zinc ion binding / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human)![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.14 Å | |||||||||
Authors | Zhou, D. / Ren, J. / Stuart, D. | |||||||||
| Funding support | United Kingdom, China, 2items
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Citation | Journal: Cell / Year: 2021Title: Antibody evasion by the P.1 strain of SARS-CoV-2. Authors: Dejnirattisai, W. / Zhou, D. / Supasa, P. / Liu, C. / Mentzer, A.J. / Ginn, H.M. / Zhao, Y. / Duyvesteyn, H.M.E. / Tuekprakhon, A. / Nutalai, R. / Wang, B. / Lopez-Camacho, C. / Slon-Campos, ...Authors: Dejnirattisai, W. / Zhou, D. / Supasa, P. / Liu, C. / Mentzer, A.J. / Ginn, H.M. / Zhao, Y. / Duyvesteyn, H.M.E. / Tuekprakhon, A. / Nutalai, R. / Wang, B. / Lopez-Camacho, C. / Slon-Campos, J. / Walter, T.S. / Skelly, D. / Costa Clemens, S.A. / Naveca, F.G. / Nascimento, V. / Nascimento, F. / Fernandes da Costa, C. / Resende, P.C. / Pauvolid-Correa, A. / Siqueira, M.M. / Dold, C. / Levin, R. / Dong, T. / Pollard, A.J. / Knight, J.C. / Crook, D. / Lambe, T. / Clutterbuck, E. / Bibi, S. / Flaxman, A. / Bittaye, M. / Belij-Rammerstorfer, S. / Gilbert, S.C. / Carroll, M.W. / Klenerman, P. / Barnes, E. / Dunachie, S.J. / Paterson, N.G. / Williams, M.A. / Hall, D.R. / Hulswit, R.J.G. / Bowden, T.A. / Fry, E.E. / Mongkolsapaya, J. / Ren, J. / Stuart, D.I. / Screaton, G.R. #1: Journal: Biorxiv / Year: 2021Title: Antibody evasion by the Brazilian P.1 strain of SARS-CoV-2 Authors: Dejnirattisai, W. / Zhou, D. / Supasa, P. / Liu, C. / Mentzer, A.J. / Ginn, H.M. / Zhao, Y. / Duyvesteyn, H.M. / Tuekprakhon, A. / Nutalai, R. / Wang, B. / Paesen, G.C. / Lopez-Camacho, C. / ...Authors: Dejnirattisai, W. / Zhou, D. / Supasa, P. / Liu, C. / Mentzer, A.J. / Ginn, H.M. / Zhao, Y. / Duyvesteyn, H.M. / Tuekprakhon, A. / Nutalai, R. / Wang, B. / Paesen, G.C. / Lopez-Camacho, C. / Slon-Campos, J. / Walter, T.S. / Skelly, D. / Clemens, S.A.C. / Naveca, F.G. / Nascimento, V. / Nascimento, F. / Dold, C. / Levin, R. / Dong, T. / Pollard, A.J. / Knight, J.C. / Crook, D. / Lambe, T. / Clutterbuck, E. / Bibi, S. / Flaxman, A. / Bittaye, M. / Belij-Rammerstorfer, S. / Gilbert, S. / Carroll, M.W. / Klenerman, P. / Barnes, E. / Dunachie, S.J. / Paterson, N.G. / Williams, M.A. / Hall, D.R. / Hulswit, R.J.G. / Bowden, T.A. / Fry, E.E. / Mongkolsapaya, J. / Ren, J. / Stuart, D.I. / Screaton, G.R. | |||||||||
| 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 | 7nxc.cif.gz | 403.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7nxc.ent.gz | 274.2 KB | Display | PDB format |
| PDBx/mmJSON format | 7nxc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7nxc_validation.pdf.gz | 464.6 KB | Display | wwPDB validaton report |
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| Full document | 7nxc_full_validation.pdf.gz | 471.8 KB | Display | |
| Data in XML | 7nxc_validation.xml.gz | 28.5 KB | Display | |
| Data in CIF | 7nxc_validation.cif.gz | 38.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nx/7nxc ftp://data.pdbj.org/pub/pdb/validation_reports/nx/7nxc | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7nx6C ![]() 7nx7C ![]() 7nx8C ![]() 7nx9C ![]() 7nxaC ![]() 7nxbC ![]() 6lzgS C: citing same article ( S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 70139.758 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACE2, UNQ868/PRO1885 / Production host: Homo sapiens (human) / References: UniProt: Q9BYF1 | ||||
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| #2: Protein | Mass: 23171.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: S, 2 / Production host: Homo sapiens (human) / References: UniProt: P0DTC2 | ||||
| #3: Sugar | ChemComp-NAG / Has ligand of interest | N | 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: 3.24 Å3/Da / Density % sol: 62.06 % |
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| Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1 M Imidazole pH 7.0 and 20% w/v Polyethylene glycol 6,000 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å |
| Detector | Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Feb 23, 2021 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9762 Å / Relative weight: 1 |
| Reflection | Resolution: 3.14→70 Å / Num. obs: 22273 / % possible obs: 100 % / Redundancy: 25.7 % / Biso Wilson estimate: 87.49 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.5 / Rpim(I) all: 0.1 / Net I/σ(I): 5.3 |
| Reflection shell | Resolution: 3.14→3.19 Å / Num. unique obs: 1047 / CC1/2: 0.31 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 6LZG Resolution: 3.14→69.62 Å / SU ML: 0.4856 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.4576 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 90.4 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.14→69.62 Å
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| Refine LS restraints |
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| 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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About Yorodumi



Homo sapiens (human)
X-RAY DIFFRACTION
United Kingdom,
China, 2items
Citation
















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