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- PDB-2snv: THE REFINED STRUCTURE OF SINDBIS VIRUS CORE PROTEIN IN COMPARISON... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2snv | ||||||
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Title | THE REFINED STRUCTURE OF SINDBIS VIRUS CORE PROTEIN IN COMPARISON WITH OTHER CHYMOTRYPSIN-LIKE SERINE PROTEINASE STRUCTURES | ||||||
![]() | SINDBIS VIRUS COAT PROTEIN | ||||||
![]() | VIRAL 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 | ![]() | ||||||
![]() | Tong, L. / Rossmann, M.G. | ||||||
![]() | ![]() 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. #1: ![]() 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. #2: ![]() 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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Remark 700 | SHEET THE STRAND ASSIGNMENTS OF THE SHEET RECORDS ARE TENTATIVE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.9 KB | Display | ![]() |
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PDB format | ![]() | 27.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367 KB | Display | ![]() |
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Full document | ![]() | 378.1 KB | Display | |
Data in XML | ![]() | 6.1 KB | Display | |
Data in CIF | ![]() | 8.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 16545.631 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.69 Å3/Da / Density % sol: 54.34 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.3 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Num. obs: 3779 / Num. measured all: 17265 / Rmerge(I) obs: 0.063 |
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Processing
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Refinement | Rfactor Rwork: 0.2 / Rfactor obs: 0.2 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 6 Å / Num. reflection obs: 3229 / Rfactor obs: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 27.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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