+Open data
-Basic information
Entry | Database: PDB / ID: 1cqq | ||||||
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Title | TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR | ||||||
Components | TYPE 2 RHINOVIRUS 3C PROTEASE | ||||||
Keywords | HYDROLASE / VIRAL PROTEIN | ||||||
Function / homology | Function and homology information symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / ribonucleoside triphosphate phosphatase activity / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / ribonucleoside triphosphate phosphatase activity / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / RNA helicase activity / DNA replication / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / host cell nucleus / structural molecule activity / virion attachment to host cell / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Human rhinovirus 2 | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.85 Å | ||||||
Authors | Matthews, D. / Ferre, R.A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 Title: Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Authors: Matthews, D.A. / Dragovich, P.S. / Webber, S.E. / Fuhrman, S.A. / Patick, A.K. / Zalman, L.S. / Hendrickson, T.F. / Love, R.A. / Prins, T.J. / Marakovits, J.T. / Zhou, R. / Tikhe, J. / Ford, ...Authors: Matthews, D.A. / Dragovich, P.S. / Webber, S.E. / Fuhrman, S.A. / Patick, A.K. / Zalman, L.S. / Hendrickson, T.F. / Love, R.A. / Prins, T.J. / Marakovits, J.T. / Zhou, R. / Tikhe, J. / Ford, C.E. / Meador, J.W. / Ferre, R.A. / Brown, E.L. / Binford, S.L. / Brothers, M.A. / DeLisle, D.M. / Worland, S.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cqq.cif.gz | 64.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cqq.ent.gz | 52.5 KB | Display | PDB format |
PDBx/mmJSON format | 1cqq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cq/1cqq ftp://data.pdbj.org/pub/pdb/validation_reports/cq/1cqq | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 19981.662 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 2 / Genus: Rhinovirus / Species: Human rhinovirus ARhinovirus / References: UniProt: P04936 |
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#2: Chemical | ChemComp-AG7 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43.98 % | ||||||||||||||||||||
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Crystal grow | Temperature: 286 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 20% PEG10K, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 13K | ||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 8, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→20 Å / Num. all: 14527 / Num. obs: 13981 / % possible obs: 89.2 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.048 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.231 / % possible all: 48.7 |
Reflection | *PLUS Rmerge(I) obs: 0.019 |
-Processing
Software |
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Refinement | Resolution: 1.85→10 Å / σ(F): 1.5 / σ(I): 1.5 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1.85→10 Å
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / σ(F): 1.5 | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||
Refine LS restraints | *PLUS
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