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Open data
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Basic information
Entry | Database: PDB / ID: 1svr | ||||||
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Title | STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION | ||||||
![]() | SEVERIN | ||||||
![]() | ACTIN-BINDING | ||||||
Function / homology | ![]() actin filament severing activity / actin filament fragmentation / Neutrophil degranulation / actin filament severing / barbed-end actin filament capping / actin polymerization or depolymerization / actin filament bundle assembly / actin monomer binding / phosphatidylinositol-4,5-bisphosphate binding / phagocytic vesicle ...actin filament severing activity / actin filament fragmentation / Neutrophil degranulation / actin filament severing / barbed-end actin filament capping / actin polymerization or depolymerization / actin filament bundle assembly / actin monomer binding / phosphatidylinositol-4,5-bisphosphate binding / phagocytic vesicle / calcium-dependent protein binding / actin filament binding / actin cytoskeleton / calcium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Schnuchel, A. / Holak, T.A. | ||||||
![]() | ![]() Title: Structure of severin domain 2 in solution. Authors: Schnuchel, A. / Wiltscheck, R. / Eichinger, L. / Schleicher, M. / Holak, T.A. #1: ![]() Title: Characterization of Actin-and Lipid-Binding Domains in Severin, a Ca(2+)-Dependent F-Actin Fragmenting Protein Authors: Eichinger, L. / Schleicher, M. #2: ![]() Title: Severin, Gelsolin, and Villin Share a Homologous Sequence in Regions Presumed to Contain F-Actin Severing Domains Authors: Andre, E. / Lottspeich, F. / Schleicher, M. / Noegel, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.6 KB | Display | ![]() |
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PDB format | ![]() | 31.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.7 KB | Display | ![]() |
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Full document | ![]() | 366 KB | Display | |
Data in XML | ![]() | 6.9 KB | Display | |
Data in CIF | ![]() | 8.8 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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NMR ensembles |
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Components
#1: Protein | Mass: 12260.842 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: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
NMR ensemble | Conformers submitted total number: 1 |
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