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- PDB-6psi: 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: 6psi | ||||||
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Title | Structural Basis for Client Recognition and Activity of Hsp40 Chaperones | ||||||
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![]() | CHAPERONE / 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. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 6.8 MB | Display | ![]() |
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PDB format | ![]() | 5.9 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 467 KB | Display | ![]() |
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Full document | ![]() | 950.1 KB | Display | |
Data in XML | ![]() | 372.8 KB | Display | |
Data in CIF | ![]() | 577.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6pptC ![]() 6pq2C ![]() 6pqeC ![]() 6pqmC ![]() 6priC ![]() 6prjC ![]() 6prpC ![]() 6prqC 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: 31023.424 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: HB8 / ATCC 27634 / DSM 579 / Gene: dnaJ2, TTHA1489 / Production host: ![]() ![]() #2: Protein | | Mass: 49492.367 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: phoA, ACU57_12080, AUQ13_18595, BANRA_02023, BANRA_03586, BET08_14335, BHF46_20915, BUE81_15475, C4J69_09555, C5N07_12695, CA593_01230, D0X26_07375, D3821_12940, DNQ41_05820, EAI52_02910, ...Gene: phoA, ACU57_12080, AUQ13_18595, BANRA_02023, BANRA_03586, BET08_14335, BHF46_20915, BUE81_15475, C4J69_09555, C5N07_12695, CA593_01230, D0X26_07375, D3821_12940, DNQ41_05820, EAI52_02910, EC3234A_4c00530, EC3426_01222, ECTO6_03716, ED648_16735, EEP23_01005, EL75_3367, EL79_3462, EL80_3416, NCTC13462_01945, NCTC9037_03964, NCTC9062_04458, RK56_026750, SAMEA3753300_00450, UN91_18770 Production host: ![]() ![]() References: UniProt: A0A086VD57, UniProt: P00634*PLUS, 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 | Type: solution Contents: 1 mM [U-100% 13C; U-100% 15N; U-80% 2H] PhoA_DnaJ, 75 mM potassium chloride, 20 mM potassium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O Details: Highly deuterated selectively ILVMAT methyl labeled Label: NCD_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 mM / Label: conditions_1 / pH: 7 / Pressure: 1 atm / Temperature: 25 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 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |