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Open data
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Basic information
Entry | Database: PDB / ID: 1f8b | |||||||||
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Title | Native Influenza Virus Neuraminidase in Complex with NEU5AC2EN | |||||||||
![]() | NEURAMINIDASE | |||||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / neuraminidase / hydrolase / influenza protein / glycosylated protein / DANA / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | ![]() exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / exo-alpha-sialidase / viral budding from plasma membrane / carbohydrate metabolic process / host cell plasma membrane / virion membrane / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Smith, B.J. / Colman, P.M. / Von Itzstein, M. / Danylec, B. / Varghese, J.N. | |||||||||
![]() | ![]() Title: Analysis of inhibitor binding in influenza virus neuraminidase. Authors: Smith, B.J. / Colman, P.M. / Von Itzstein, M. / Danylec, B. / Varghese, J.N. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98 KB | Display | ![]() |
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PDB format | ![]() | 77.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 21.2 KB | Display | |
Data in CIF | ![]() | 31.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 43723.770 Da / Num. of mol.: 1 Fragment: INTEGRAL MEMBRANE PROTEIN, MEMBRANE STALK CLEAVED BY PRONASE RELEASING FULLY ACTIVE RESIDUES 82-468. Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Genus: Influenzavirus A / Species: Influenza A virus / Strain: A/TERN/AUSTRALIA/G70C/75 / Genus (production host): Influenzavirus A / Production host: ![]() ![]() References: GenBank: 324880, UniProt: P03472*PLUS, exo-alpha-sialidase |
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-Sugars , 4 types, 4 molecules ![](data/chem/img/NAG.gif)
A![](data/chem/img/DAN.gif)
![](data/chem/img/DAN.gif)
#2: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Sugar | ChemComp-NAG / |
#6: Sugar |
-Non-polymers , 2 types, 348 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.83 Å3/Da / Density % sol: 56.47 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.9 Details: phosphate, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 293.0 K | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Laver, W.G., (1984) Virology, 137, 314. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Dec 20, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 30479 / % possible obs: 75 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.071 / Net I/σ(I): 10.6 |
Reflection | *PLUS Highest resolution: 1.8 Å |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 2 Å / % possible obs: 92.2 % |
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Processing
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Refinement | Highest resolution: 1.8 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_plane_restr / Dev ideal: 0.88 |