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- PDB-1dro: NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN -

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Basic information

Entry
Database: PDB / ID: 1dro
TitleNMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN
ComponentsBETA-SPECTRIN
KeywordsCYTOSKELETON
Function / homology
Function and homology information


long-term strengthening of neuromuscular junction / spectrosome / maintenance of presynaptic active zone structure / fusome / photoreceptor cell axon guidance / regulation of plasma membrane organization / COPI-mediated anterograde transport / spectrin / neuromuscular synaptic transmission / negative regulation of microtubule depolymerization ...long-term strengthening of neuromuscular junction / spectrosome / maintenance of presynaptic active zone structure / fusome / photoreceptor cell axon guidance / regulation of plasma membrane organization / COPI-mediated anterograde transport / spectrin / neuromuscular synaptic transmission / negative regulation of microtubule depolymerization / actin filament capping / axon midline choice point recognition / ankyrin binding / regulation of synapse organization / lateral plasma membrane / phosphatidylinositol-4,5-bisphosphate binding / axonogenesis / axon guidance / neuromuscular junction / structural constituent of cytoskeleton / nervous system development / actin binding / microtubule binding / calmodulin binding / axon / plasma membrane
Similarity search - Function
Pleckstrin homology domain, spectrin-type / Pleckstrin homology domain 9 / Pleckstrin homology domain / Spectrin, beta subunit / Spectrin repeat / Spectrin repeat / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Spectrin/alpha-actinin ...Pleckstrin homology domain, spectrin-type / Pleckstrin homology domain 9 / Pleckstrin homology domain / Spectrin, beta subunit / Spectrin repeat / Spectrin repeat / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Spectrin/alpha-actinin / Spectrin repeats / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / PH domain / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / PH-like domain superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
Biological speciesDrosophila melanogaster (fruit fly)
MethodSOLUTION NMR
AuthorsZhang, P. / Talluri, S. / Deng, H. / Branton, D. / Wagner, G.
CitationJournal: Structure / Year: 1995
Title: Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin.
Authors: Zhang, P. / Talluri, S. / Deng, H. / Branton, D. / Wagner, G.
History
DepositionSep 29, 1995Processing site: BNL
Revision 1.0Apr 3, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BETA-SPECTRIN


Theoretical massNumber of molelcules
Total (without water)13,5831
Polymers13,5831
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / -
Representative

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Components

#1: Protein BETA-SPECTRIN


Mass: 13583.059 Da / Num. of mol.: 1 / Fragment: PLECKSTRIN HOMOLOGY DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Description: EXPRESSION VECTOR USED WAS PGEX-2T / Organ: FRUIT / Production host: Escherichia coli (E. coli) / References: UniProt: Q00963

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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

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Processing

NMR softwareName: DGII / Developer: HAVEL / Classification: refinement
NMR ensembleConformers submitted total number: 15

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