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Yorodumi- PDB-5xla: The structure of hemagglutinin G228S mutant from an avian-origin ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5xla | ||||||
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Title | The structure of hemagglutinin G228S mutant from an avian-origin H4N6 influenza virus in complex with human receptor analog LSTc | ||||||
Components | Hemagglutinin | ||||||
Keywords | VIRAL PROTEIN / H4 hemagglutinin / influenza virus / receptor binding | ||||||
Function / homology | Function and homology information viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane Similarity search - Function | ||||||
Biological species | Influenza A virus | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Song, H. / Qi, J. / Gao, G.F. | ||||||
Citation | Journal: Cell Rep / Year: 2017 Title: Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4 Authors: Song, H. / Qi, J. / Xiao, H. / Bi, Y. / Zhang, W. / Xu, Y. / Wang, F. / Shi, Y. / Gao, G.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xla.cif.gz | 418.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xla.ent.gz | 345.4 KB | Display | PDB format |
PDBx/mmJSON format | 5xla.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xl/5xla ftp://data.pdbj.org/pub/pdb/validation_reports/xl/5xla | HTTPS FTP |
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-Related structure data
Related structure data | 5xl1C 5xl2C 5xl3C 5xl4C 5xl5C 5xl6C 5xl7C 5xl8C 5xl9C 5xlbC 5xlcC 5xldC 1ha0S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 56320.773 Da / Num. of mol.: 2 / Fragment: UNP residues 17-519 / Mutation: G228S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Influenza A virus / Strain: A/Duck/Czechoslovakia/1956 H4N6 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: A3KF09, UniProt: P19696*PLUS #2: Sugar | #3: Sugar | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.97 Å3/Da / Density % sol: 58.65 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 / Details: 0.1 M Bis-Tris (pH 6.5) and 20% (w/v) PEG 1,500 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 29, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 79407 / % possible obs: 100 % / Redundancy: 10.4 % / Net I/σ(I): 20.7 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 10.5 % / Rmerge(I) obs: 0.791 / Mean I/σ(I) obs: 3.4 / Rsym value: 0.791 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1HA0 Resolution: 2.1→43.266 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.75
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→43.266 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 27.427 Å / Origin y: 338.7767 Å / Origin z: 748.0833 Å
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Refinement TLS group | Selection details: all |