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Yorodumi- PDB-1zba: Foot-and-Mouth Disease virus serotype A1061 complexed with oligos... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zba | |||||||||
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Title | Foot-and-Mouth Disease virus serotype A1061 complexed with oligosaccharide receptor. | |||||||||
Components | (Coat protein ...) x 4 | |||||||||
Keywords | VIRUS / oligosaccharide receptor / VIRUS/VIRAL PROTEIN / Icosahedral virus | |||||||||
Function / homology | Function and homology information : / L-peptidase / modulation by virus of host chromatin organization / positive stranded viral RNA replication / RNA-protein covalent cross-linking / : / : / ribonucleoside triphosphate phosphatase activity / picornain 3C / T=pseudo3 icosahedral viral capsid ...: / L-peptidase / modulation by virus of host chromatin organization / positive stranded viral RNA replication / RNA-protein covalent cross-linking / : / : / ribonucleoside triphosphate phosphatase activity / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / regulation of translation / clathrin-dependent endocytosis of virus by host cell / RNA helicase activity / viral protein processing / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / virion attachment to host cell / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane Similarity search - Function | |||||||||
Biological species | Foot-and-mouth disease virus | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | |||||||||
Authors | Fry, E.E. / Newman, J.W. / Curry, S. / Najjam, S. / Jackson, T. / Blakemore, W. / Lea, S.M. / Miller, L. / Burman, A. / King, A.M. / Stuart, D.I. | |||||||||
Citation | Journal: J.Gen.Virol. / Year: 2005 Title: Structure of Foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation. Authors: Fry, E.E. / Newman, J.W. / Curry, S. / Najjam, S. / Jackson, T. / Blakemore, W. / Lea, S.M. / Miller, L. / Burman, A. / King, A.M. / Stuart, D.I. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zba.cif.gz | 159.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zba.ent.gz | 124 KB | Display | PDB format |
PDBx/mmJSON format | 1zba.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zb/1zba ftp://data.pdbj.org/pub/pdb/validation_reports/zb/1zba | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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5 |
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6 |
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Unit cell |
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Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
-Coat protein ... , 4 types, 4 molecules 1234
#1: Protein | Mass: 23293.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Foot-and-mouth disease virus / Genus: Aphthovirus / References: UniProt: Q84769, UniProt: P03306*PLUS |
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#2: Protein | Mass: 24678.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Foot-and-mouth disease virus / Genus: Aphthovirus / References: UniProt: Q84769, UniProt: P03306*PLUS |
#3: Protein | Mass: 24233.992 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Foot-and-mouth disease virus / Genus: Aphthovirus / References: UniProt: Q84769, UniProt: P03306*PLUS |
#4: Protein | Mass: 8794.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Foot-and-mouth disease virus / Genus: Aphthovirus / References: UniProt: Q84769, UniProt: P03306*PLUS |
-Sugars / Non-polymers , 2 types, 451 molecules
#5: Polysaccharide | 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid- ...2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 452651 / Rmerge(I) obs: 0.135 |
-Processing
Software | Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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