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Open data
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Basic information
Entry | Database: PDB / ID: 1qqp | ||||||||||||
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Title | FOOT-AND-MOUTH DISEASE VIRUS/ OLIGOSACCHARIDE RECEPTOR COMPLEX. | ||||||||||||
![]() | (PROTEIN (GENOME ...) x 4 | ||||||||||||
![]() | VIRUS / HEPARAN SULPHATE / VIRUS-RECEPTOR INTERACTIONS/PROTEIN-CARBOHYDRATE INTERACTIONS / VIRUS/VIRAL PROTEIN / Icosahedral virus | ||||||||||||
Function / homology | ![]() L-peptidase / suppression by virus of host type I interferon production / modulation by virus of host chromatin organization / 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 ...L-peptidase / suppression by virus of host type I interferon production / modulation by virus of host chromatin organization / 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 / molecular adaptor activity / RNA helicase activity / host cell endoplasmic reticulum membrane / 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 / host cell nucleus / virion attachment to host cell / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Fry, E.E. / Lea, S.M. / Jackson, T. / Newman, J.W.I. / Ellard, F.M. / Blakemore, W.E. / Abu-Ghazaleh, R. / Samuel, A. / King, A.M.Q. / Stuart, D.I. | ||||||||||||
![]() | ![]() Title: The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. Authors: Fry, E.E. / Lea, S.M. / Jackson, T. / Newman, J.W. / Ellard, F.M. / Blakemore, W.E. / Abu-Ghazaleh, R. / Samuel, A. / King, A.M. / Stuart, D.I. #1: ![]() Title: Structure of a Major Immunogenic Site on Foot-and-Mouth Disease Virus Authors: Logan, D. / Abu-Ghazaleh, R. / Blakemore, W. / Curry, S. / Jackson, T. / King, A. / Lea, S. / Lewis, R. / Stuart, D. / Fry, E. #2: ![]() Title: The Three-Dimensional Structure of Foot-and-Mouth Disease Virus at 2.9 Angstroms Resolution Authors: Acharya, R. / Fry, E. / Stuart, D. / Fox, G. / Rowlands, D. / Brown, F. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 165.6 KB | Display | ![]() |
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PDB format | ![]() | 128.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 488.9 KB | Display | ![]() |
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Full document | ![]() | 512.8 KB | Display | |
Data in XML | ![]() | 18.5 KB | Display | |
Data in CIF | ![]() | 30.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bttS 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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1 | ![]()
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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
-PROTEIN (GENOME ... , 4 types, 4 molecules 1234
#1: Protein | Mass: 23828.184 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: GROWN IN BHK CELLS / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 24373.455 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: GROWN IN BHK CELLS / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 23860.830 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: GROWN IN BHK CELLS / Source: (natural) ![]() ![]() |
#4: Protein | Mass: 8778.129 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: GROWN IN BHK CELLS / Source: (natural) ![]() ![]() |
-Sugars / Non-polymers , 2 types, 632 molecules ![](data/chem/img/HOH.gif)
#5: Polysaccharide | 2-O-sulfo-alpha-L-gulopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose- ...2-O-sulfo-alpha-L-gulopyranuronic acid-(1-4)-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-(1-4)-2-O-sulfo-alpha-L-gulopyranuronic acid Source method: isolated from a genetically manipulated source |
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#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | pH: 7.5 / Details: pH 7.50 | |||||||||||||||
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Crystal grow | *PLUS pH: 7.6 / Method: microdialysis | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE |
Radiation | Monochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→12 Å / Num. obs: 2070213 / % possible obs: 91 % / Redundancy: 4.3 % / Rmerge(I) obs: 0.143 |
Reflection shell | *PLUS % possible obs: 77.4 % |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: PDB ENTRY 1BTT Resolution: 1.9→12 Å / Data cutoff high absF: 0 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / σ(F): 0 Details: THE DENSITY WAS TOO WEAK TO MODEL THE SIDE CHAINS ACCURATELY FOR CHAIN 1 RESIDUES ARG 157 AND THR 158.
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Refinement step | Cycle: LAST / Resolution: 1.9→12 Å
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Refine LS restraints |
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