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- PDB-1svq: STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION -

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Basic information

Entry
Database: PDB / ID: 1svq
TitleSTRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
ComponentsSEVERIN
KeywordsACTIN-BINDING
Function / homology
Function and homology information


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 / phagocytic vesicle / phosphatidylinositol-4,5-bisphosphate binding ...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 / phagocytic vesicle / phosphatidylinositol-4,5-bisphosphate binding / calcium-dependent protein binding / actin filament binding / actin cytoskeleton / calcium ion binding / cytoplasm
Similarity search - Function
Villin/Gelsolin / Gelsolin homology domain / Severin / Severin / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesDictyostelium discoideum (eukaryote)
MethodSOLUTION NMR
AuthorsSchnuchel, A. / Holak, T.A.
Citation
Journal: J.Mol.Biol. / Year: 1995
Title: Structure of severin domain 2 in solution.
Authors: Schnuchel, A. / Wiltscheck, R. / Eichinger, L. / Schleicher, M. / Holak, T.A.
#1: Journal: Biochemistry / Year: 1992
Title: Characterization of Actin-and Lipid-Binding Domains in Severin, a Ca(2+)-Dependent F-Actin Fragmenting Protein
Authors: Eichinger, L. / Schleicher, M.
#2: Journal: J.Biol.Chem. / Year: 1988
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
DepositionOct 12, 1994Processing site: BNL
Revision 1.0Feb 7, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Oct 23, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure viewerMolecule:
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Assembly

Deposited unit
A: SEVERIN


Theoretical massNumber of molelcules
Total (without water)12,2611
Polymers12,2611
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein SEVERIN


Mass: 12260.842 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Dictyostelium discoideum (eukaryote) / References: UniProt: P10733
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 20

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