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- PDB-1hdj: HUMAN HSP40 (HDJ-1), NMR -

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Basic information

Entry
Database: PDB / ID: 1hdj
TitleHUMAN HSP40 (HDJ-1), NMR
ComponentsHUMAN HSP40
KeywordsMOLECULAR CHAPERONE
Function / homology
Function and homology information


sperm head / negative regulation of inclusion body assembly / positive regulation of ATP-dependent activity / transcription regulator inhibitor activity / ATPase activator activity / chaperone cofactor-dependent protein refolding / HSF1-dependent transactivation / response to unfolded protein / Regulation of HSF1-mediated heat shock response / Attenuation phase ...sperm head / negative regulation of inclusion body assembly / positive regulation of ATP-dependent activity / transcription regulator inhibitor activity / ATPase activator activity / chaperone cofactor-dependent protein refolding / HSF1-dependent transactivation / response to unfolded protein / Regulation of HSF1-mediated heat shock response / Attenuation phase / regulation of cellular response to heat / forebrain development / protein folding chaperone / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Hsp70 protein binding / MAPK6/MAPK4 signaling / transcription corepressor activity / unfolded protein binding / protein-folding chaperone binding / cellular response to heat / ATPase binding / dendritic spine / postsynaptic density / cadherin binding / neuronal cell body / glutamatergic synapse / nucleolus / negative regulation of transcription by RNA polymerase II / extracellular exosome / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
: / DnaJ domain / HSP40/DnaJ peptide-binding / Chaperone DnaJ, C-terminal / DnaJ C terminal domain / Nt-dnaJ domain signature. / DnaJ domain, conserved site / DnaJ domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. ...: / DnaJ domain / HSP40/DnaJ peptide-binding / Chaperone DnaJ, C-terminal / DnaJ C terminal domain / Nt-dnaJ domain signature. / DnaJ domain, conserved site / DnaJ domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Chaperone J-domain superfamily / DnaJ domain / Helix Hairpins / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
DnaJ homolog subfamily B member 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsQian, Y.Q. / Patel, D. / Hartl, F.-U. / Mccoll, D.J.
CitationJournal: J.Mol.Biol. / Year: 1996
Title: Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.
Authors: Qian, Y.Q. / Patel, D. / Hartl, F.U. / McColl, D.J.
History
DepositionMay 9, 1996Processing site: BNL
Revision 1.0Nov 8, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HUMAN HSP40


Theoretical massNumber of molelcules
Total (without water)8,9191
Polymers8,9191
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein HUMAN HSP40 / HDJ-1


Mass: 8918.938 Da / Num. of mol.: 1 / Fragment: J-DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P25685

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 5.8 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

SoftwareName: AMBER / Classification: refinement
NMR softwareName: DIANA / Developer: GUNTERT,BRAUN,WUTHRICH / Classification: refinement
NMR ensembleConformers submitted total number: 20

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