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- PDB-6prq: Structural Basis for Client Recognition and Activity of Hsp40 Cha... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6prq | ||||||
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Title | Structural Basis for Client Recognition and Activity of Hsp40 Chaperones | ||||||
![]() | Alkaline phosphatase,Chaperone protein DnaJ 2 fusion | ||||||
![]() | CHAPERONE / HYDROLASE / Client Recognition | ||||||
Function / homology | ![]() oxidoreductase activity, acting on phosphorus or arsenic in donors / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / chaperone cofactor-dependent protein refolding / dephosphorylation / protein dephosphorylation / unfolded protein binding / outer membrane-bounded periplasmic space ...oxidoreductase activity, acting on phosphorus or arsenic in donors / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / chaperone cofactor-dependent protein refolding / dephosphorylation / protein dephosphorylation / unfolded protein binding / outer membrane-bounded periplasmic space / protein refolding / DNA replication / periplasmic space / magnesium ion binding / zinc ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Jiang, Y. / Rossi, P. / Kalodimos, C.G. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for client recognition and activity of Hsp40 chaperones. Authors: Jiang, Y. / Rossi, P. / Kalodimos, C.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 910.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 404 KB | Display | ![]() |
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Full document | ![]() | 492.4 KB | Display | |
Data in XML | ![]() | 58.9 KB | Display | |
Data in CIF | ![]() | 81.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6pptC ![]() 6pq2C ![]() 6pqeC ![]() 6pqmC ![]() 6priC ![]() 6prjC ![]() 6prpC ![]() 6psiC C: citing same article ( |
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Similar 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: 16625.180 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Strain: K12, HB8 / ATCC 27634 / DSM 579 / Gene: phoA, b0383, JW0374, dnaJ2, TTHA1489 / Production host: ![]() ![]() References: UniProt: P00634, UniProt: Q56237, alkaline phosphatase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 100 mM / Label: conditions_1 / pH: 7 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE NEO / Manufacturer: Bruker / Model: AVANCE NEO / Field strength: 700 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 / Details: restrained MD in H2O | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |