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- PDB-1rui: RHINOVIRUS 14 MUTANT S1223G COMPLEXED WITH ANTIVIRAL COMPOUND WIN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rui | |||||||||
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Title | RHINOVIRUS 14 MUTANT S1223G COMPLEXED WITH ANTIVIRAL COMPOUND WIN 52084 | |||||||||
![]() | (RHINOVIRUS 14) x 4 | |||||||||
![]() | VIRUS / RHINOVIRUS COAT PROTEIN / Icosahedral virus | |||||||||
Function / homology | ![]() lysis of host organelle 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 / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase ...lysis of host organelle 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 / 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 / DNA replication / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Hadfield, A. / Oliveira, M.A. / Kim, K.H. / Minor, I. / Kremer, M.J. / Heinz, B.A. / Shepard, D. / Pevear, D.C. / Rueckert, R.R. / Rossmann, M.G. | |||||||||
![]() | ![]() Title: Structural studies on human rhinovirus 14 drug-resistant compensation mutants. Authors: Hadfield, A.T. / Oliveira, M.A. / Kim, K.H. / Minor, I. / Kremer, M.J. / Heinz, B.A. / Shepard, D. / Pevear, D.C. / Rueckert, R.R. / Rossmann, M.G. #1: ![]() Title: Win 52035-2 Inhibits Both Attachment and Eclipse of Human Rhinovirus 14 Authors: Shepard, D.A. / Heinz, B.A. / Rueckert, R.R. #2: ![]() Title: Analysis of the Structure of a Common Cold Virus, Human Rhinovirus 14, Refined at a Resolution of 3.0 Angstroms Authors: Arnold, E. / Rossmann, M.G. #3: ![]() Title: Three Dimensional Structures of Drug-Resistant Mutants of Human Rhinovirus 14 Authors: Badger, J. / Krishnaswamy, S. / Kremer, M.J. / Oliveira, M.A. / Rossmann, M.G. / Heinz, B.A. / Rueckert, R.R. / Dutko, F.J. / Mckinlay, M.A. #4: ![]() Title: Structural Analysis of Antiviral Agents that Interact with the Capsid of Human Rhinoviruses Authors: Badger, J. / Minor, I. / Oliveira, M.A. / Smith, T.J. / Rossmann, M.G. #5: ![]() Title: Genetics and Molecular Basis for Resistance of Human Rhinovirus 14 to an Antiviral Drug Authors: Heinz, B.A. / Rueckert, R.R. / Shepard, D.A. / Dutko, F.J. / Mckinlay, M.A. / Fancher, M. / Rossmann, M.G. / Badger, J. / Smith, T.J. #6: ![]() Title: The Use of Molecular Replacement Phases for the Refinement of the Human Rhinovirus 14 Structure Authors: Arnold, E. / Rossmann, M.G. #7: ![]() Title: Structural Analysis of a Series of Antiviral Agents Complexed with Human Rhinovirus 14 Authors: Badger, J. / Minor, I. / Kremer, M.J. / Oliveira, M.A. / Smith, T.J. / Griffith, J.P. / Guerin, D.M.A. / Krishnaswamy, S. / Luo, M. / Rossmann, M.G. / Mckinlay, M.A. / Diana, G.D. / Dutko, F. ...Authors: Badger, J. / Minor, I. / Kremer, M.J. / Oliveira, M.A. / Smith, T.J. / Griffith, J.P. / Guerin, D.M.A. / Krishnaswamy, S. / Luo, M. / Rossmann, M.G. / Mckinlay, M.A. / Diana, G.D. / Dutko, F.J. / Fancher, M. / Rueckert, R.R. / Heinz, B.A. #8: ![]() Title: The Structure Determination of a Common Cold Virus, Human Rhinovirus 14 Authors: Arnold, E. / Vriend, G. / Luo, M. / Griffith, J.P. / Kamer, G. / Erickson, J.W. / Johnson, J.E. / Rossmann, M.G. #9: ![]() Title: The Site of Attachment in Human Rhinovirus 14 for Antiviral Agents that Inhibit Uncoating Authors: Smith, T.J. / Kremer, M.J. / Luo, M. / Vriend, G. / Arnold, E. / Kamer, G. / Rossmann, M.G. / Mckinlay, M.A. / Diana, G.D. / Otto, M.J. #10: ![]() Title: Structure of a Human Common Cold Virus and Functional Relationship to Other Picornaviruses Authors: Rossmann, M.G. / Arnold, E. / Erickson, J.W. / Frankenberger, E.A. / Griffith, J.P. / Hecht, H.-J. / Johnson, J.E. / Kamer, G. / Luo, M. / Mosser, A.G. / Rueckert, R.R. / Sherry, B. / Vriend, G. #11: ![]() Title: Virion Orientation in Cubic Crystals of the Human Common Cold Virus Hrv14 Authors: Arnold, E. / Erickson, J.W. / Fout, G.S. / Frankenberger, E.A. / Hecht, H.-J. / Luo, M. / Rossmann, M.G. / Rueckert, R.R. | |||||||||
History |
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Remark 700 | SHEET THERE IS A BIFURCATED SHEET IN EACH OF CHAINS *1*, *2*, AND *3*. TO REPRESENT THIS FEATURE ...SHEET THERE IS A BIFURCATED SHEET IN EACH OF CHAINS *1*, *2*, AND *3*. TO REPRESENT THIS FEATURE REDUNDANT SHEETS ARE DEFINED. THUS SHEETS B11 AND B12 DIFFER ONLY IN STRAND 4, SHEETS B12 AND B22 DIFFER ONLY IN STRAND 4, AND SHEETS B13 AND B23 DIFFER IN STRANDS 1 AND 4 (DOUBLY BIFURCATED). |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 156.7 KB | Display | ![]() |
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PDB format | ![]() | 117.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1rucC ![]() 1rudC ![]() 1rueC ![]() 1rufC ![]() 1rugC ![]() 1ruhC ![]() 1rujC C: citing same article ( |
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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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Atom site foot note | 1: CIS PROLINE - PRO 2 83 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 32530.521 Da / Num. of mol.: 1 / Mutation: S(1)223G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: HELA CELLS, MUTANTS FOUND BY SCREENING TECHNIQUES IN THE PRESENCE OF WIN COMPOUNDS WIN 52035 AND WIN 52084 Cell line (production host): HeLa cells / Production host: ![]() |
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#2: Protein | Mass: 28501.361 Da / Num. of mol.: 1 / Mutation: S(1)223G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: HELA CELLS, MUTANTS FOUND BY SCREENING TECHNIQUES IN THE PRESENCE OF WIN COMPOUNDS WIN 52035 AND WIN 52084 Cell line (production host): HeLa cells / Production host: ![]() |
#3: Protein | Mass: 26236.754 Da / Num. of mol.: 1 / Mutation: S(1)223G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: HELA CELLS, MUTANTS FOUND BY SCREENING TECHNIQUES IN THE PRESENCE OF WIN COMPOUNDS WIN 52035 AND WIN 52084 Cell line (production host): HeLa cells / Production host: ![]() |
#4: Protein | Mass: 7183.863 Da / Num. of mol.: 1 / Mutation: S(1)223G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: HELA CELLS, MUTANTS FOUND BY SCREENING TECHNIQUES IN THE PRESENCE OF WIN COMPOUNDS WIN 52035 AND WIN 52084 Cell line (production host): HeLa cells / Production host: ![]() |
#5: Chemical | ChemComp-W84 / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | *PLUS pH: 7.2 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
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Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: KODAK / Detector: FILM / Date: Aug 1, 1988 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.895 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. obs: 85028 / % possible obs: 17.7 % / Observed criterion σ(I): 3 / Rmerge(I) obs: 0.116 |
Reflection | *PLUS Num. measured all: 96067 |
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Processing
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Refinement | Highest resolution: 3 Å Details: CONFORMATIONAL DIFFERENCES OCCUR ONLY AT MUTATION SITE GLY 1 223 IN CHAIN 1. | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3 Å
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