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- PDB-1kxa: SINDBIS VIRUS CAPSID, (WILD-TYPE) RESIDUES 106-264, TETRAGONAL CR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1kxa | ||||||
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Title | SINDBIS VIRUS CAPSID, (WILD-TYPE) RESIDUES 106-264, TETRAGONAL CRYSTAL FORM | ||||||
![]() | SINDBIS VIRUS CAPSID PROTEIN | ||||||
![]() | VIRAL PROTEIN / SINDBIS VIRUS CAPSID PROTEIN / CHYMOTRYPSIN-LIKE SERINE PROTEINASE / WILD TYPE / COAT PROTEIN | ||||||
Function / homology | ![]() icosahedral viral capsid, spike / togavirin / T=4 icosahedral viral capsid / ubiquitin-like protein ligase binding / symbiont-mediated suppression of host toll-like receptor signaling pathway / clathrin-dependent endocytosis of virus by host cell / host cell cytoplasm / membrane fusion / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane ...icosahedral viral capsid, spike / togavirin / T=4 icosahedral viral capsid / ubiquitin-like protein ligase binding / symbiont-mediated suppression of host toll-like receptor signaling pathway / clathrin-dependent endocytosis of virus by host cell / host cell cytoplasm / membrane fusion / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / host cell nucleus / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / RNA binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Choi, H.-K. / Rossmann, M.G. | ||||||
![]() | ![]() Title: Structural analysis of Sindbis virus capsid mutants involving assembly and catalysis. Authors: Choi, H.K. / Lee, S. / Zhang, Y.P. / McKinney, B.R. / Wengler, G. / Rossmann, M.G. / Kuhn, R.J. #1: ![]() Title: Refined Structure of Sindbis Virus Core Protein and Comparison with Other Chymotrypsin-Like Serine Proteinase Structures Authors: Tong, L. / Wengler, G. / Rossmann, M.G. #2: ![]() Title: The Structure Determination of Sindbis Virus Core Protein Using Isomorphous Replacement and Molecular Replacement Averaging between Two Crystal Forms Authors: Tong, L. / Choi, H.-K. / Minor, W. / Rossmann, M.G. #3: ![]() Title: Structure of Sindbis Virus Core Protein Reveals a Chymotrypsin-Like Serine Proteinase and the Organization of the Virion Authors: Choi, H.K. / Tong, L. / Minor, W. / Dumas, P. / Boege, U. / Rossmann, M.G. / Wengler, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 41.4 KB | Display | ![]() |
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PDB format | ![]() | 28.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 408.3 KB | Display | ![]() |
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Full document | ![]() | 411.3 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 9.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kxbC ![]() 1kxcC ![]() 1kxdC ![]() 1kxeC ![]() 1kxfC ![]() 2snwC C: citing same article ( |
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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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Components
#1: Protein | Mass: 17418.680 Da / Num. of mol.: 1 / Fragment: MET 106 - ALA 264 OF THE NATIVE SINDBIS CAPSID Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P03316, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 8.5 / PH range high: 7.6 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SEALED TUBE / Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jul 3, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 2731 / % possible obs: 76.3 % / Observed criterion σ(I): 1 / Redundancy: 2.3 % / Rmerge(I) obs: 0.076 |
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 9999 Å / Num. obs: 3596 / Num. measured all: 8276 |
Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 3.2 Å / % possible obs: 27.1 % / Rmerge(I) obs: 0.237 |
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Processing
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Refinement | Resolution: 3.1→6 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 21.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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