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- PDB-1hri: STRUCTURE DETERMINATION OF ANTIVIRAL COMPOUND SCH 38057 COMPLEXED... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hri | |||||||||
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Title | STRUCTURE DETERMINATION OF ANTIVIRAL COMPOUND SCH 38057 COMPLEXED WITH HUMAN RHINOVIRUS 14 | |||||||||
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![]() | VIRUS / 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 / symbiont-mediated suppression of host gene expression / 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 | ![]() | |||||||||
![]() | Zhang, A. / Nanni, R.G. / Oren, D.A. / Arnold, E. | |||||||||
![]() | ![]() Title: Structure determination of antiviral compound SCH 38057 complexed with human rhinovirus 14. Authors: Zhang, A. / Nanni, R.G. / Li, T. / Arnold, G.F. / Oren, D.A. / Jacobo-Molina, A. / Williams, R.L. / Kamer, G. / Rubenstein, D.A. / Li, Y. / Rozhon, E. / Cox, S. / Buontempo, P. / O'Connell, ...Authors: Zhang, A. / Nanni, R.G. / Li, T. / Arnold, G.F. / Oren, D.A. / Jacobo-Molina, A. / Williams, R.L. / Kamer, G. / Rubenstein, D.A. / Li, Y. / Rozhon, E. / Cox, S. / Buontempo, P. / O'Connell, J. / Schwartz, J. / Miller, G. / Bauer, B. / Versace, R. / Pinto, P. / Ganguly, A. / Girijavallabhan, V. / Arnold, E. #1: ![]() Title: Sch 38057: A Picornavirus Capsid-Binding Molecule with Antiviral Activity After the Initial Stage of Viral Uncoating Authors: Rozhon, E. / Cox, S. / Buontempo, P. / O'Connell, J. / Slater, W. / De Martino, J. / Schwartz, J. / Miller, G. / Arnold, E. / Zhang, A. / Morrow, C. / Jablonski, S. / Pinto, P. / Versace, R. ...Authors: Rozhon, E. / Cox, S. / Buontempo, P. / O'Connell, J. / Slater, W. / De Martino, J. / Schwartz, J. / Miller, G. / Arnold, E. / Zhang, A. / Morrow, C. / Jablonski, S. / Pinto, P. / Versace, R. / Duelfer, T. / Girijavallabhan, V. #2: ![]() Title: Three-Dimensional Structure-Activity Relationships for Antiviral Agents that Interact with Picornavirus Capsids Authors: Zhang, A. / Nanni, R.G. / Oren, D.A. / Rozhon, E.J. / Arnold, E. #3: ![]() 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. #4: ![]() Title: The Use of Molecular-Replacement Phases for the Refinement of the Human Rhinovirus 14 Structure Authors: Arnold, E. / Rossmann, M.G. #5: ![]() 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. | |||||||||
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 | ![]() | 155.7 KB | Display | ![]() |
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PDB format | ![]() | 117.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 467.1 KB | Display | ![]() |
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Full document | ![]() | 549.4 KB | Display | |
Data in XML | ![]() | 28.7 KB | Display | |
Data in CIF | ![]() | 40 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: RESIDUE PRO 2 83 IS A CIS PROLINE. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 32560.549 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 28501.361 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Protein | Mass: 26236.754 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#4: Protein | Mass: 7183.863 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#5: Chemical | ChemComp-S57 / |
Sequence details | THE STRAIN USED IN THIS STUDY HAS A MUTATION AT RESIDUE 170 OF CHAIN 2. IN THE NATIVE VIRUS THIS ...THE STRAIN USED IN THIS STUDY HAS A MUTATION AT RESIDUE 170 OF CHAIN 2. IN THE NATIVE VIRUS THIS RESIDUE IS ILE. IN THE STRAIN USED IN THIS STUDY THIS RESIDUE IS LEU. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | *PLUS pH: 7.2 / Method: vapor diffusion, hanging dropDetails: taken from Arnold, E. et al (1984). J. Mol. Biol., 177, 417-430. | ||||||||||||||||||||||||||||||||||||||||||||||||
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Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 30 Å / Num. obs: 147740 / Rmerge(I) obs: 0.12 |
Reflection shell | *PLUS Highest resolution: 3 Å / Lowest resolution: 3.5 Å / % possible obs: 19 % / Num. unique obs: 40195 |
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Processing
Software | Name: FRODO / Classification: model building | ||||||||||||
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Refinement | Highest resolution: 3 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3 Å
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