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Yorodumi- PDB-6prq: Structural Basis for Client Recognition and Activity of Hsp40 Cha... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6prq | ||||||
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Title | Structural Basis for Client Recognition and Activity of Hsp40 Chaperones | ||||||
Components | Alkaline phosphatase,Chaperone protein DnaJ 2 fusion | ||||||
Keywords | CHAPERONE / HYDROLASE / Client Recognition | ||||||
Function / homology | Function and homology information 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 / protein dephosphorylation / unfolded protein binding / outer membrane-bounded periplasmic space / protein refolding ...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 / 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 | Escherichia coli (E. coli) Thermus thermophilus (bacteria) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Authors | Jiang, Y. / Rossi, P. / Kalodimos, C.G. | ||||||
Funding support | United States, 1items
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Citation | Journal: Science / Year: 2019 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6prq.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6prq.ent.gz | 910.8 KB | Display | PDB format |
PDBx/mmJSON format | 6prq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6prq_validation.pdf.gz | 404 KB | Display | wwPDB validaton report |
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Full document | 6prq_full_validation.pdf.gz | 492.4 KB | Display | |
Data in XML | 6prq_validation.xml.gz | 58.9 KB | Display | |
Data in CIF | 6prq_validation.cif.gz | 81.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pr/6prq ftp://data.pdbj.org/pub/pdb/validation_reports/pr/6prq | HTTPS FTP |
-Related structure data
Related structure data | 6pptC 6pq2C 6pqeC 6pqmC 6priC 6prjC 6prpC 6psiC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Escherichia coli (strain K12) (bacteria), (gene. exp.) Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (bacteria) Strain: K12, HB8 / ATCC 27634 / DSM 579 / Gene: phoA, b0383, JW0374, dnaJ2, TTHA1489 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) 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 |