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- PDB-2d9d: Solution structure of the BAG domain (275-350) of BAG-family mole... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2d9d | ||||||
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Title | Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5 | ||||||
![]() | BAG family molecular chaperone regulator 5 | ||||||
![]() | CHAPERONE / triple helix bundle / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | ![]() regulation of inclusion body assembly / junctional membrane complex / negative regulation of protein refolding / regulation of ubiquitin-protein transferase activity / adenyl-nucleotide exchange factor activity / negative regulation of ubiquitin-protein transferase activity / Golgi organization / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / Regulation of HSF1-mediated heat shock response / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway ...regulation of inclusion body assembly / junctional membrane complex / negative regulation of protein refolding / regulation of ubiquitin-protein transferase activity / adenyl-nucleotide exchange factor activity / negative regulation of ubiquitin-protein transferase activity / Golgi organization / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / Regulation of HSF1-mediated heat shock response / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / inclusion body / negative regulation of protein ubiquitination / protein folding / negative regulation of neuron projection development / protein-folding chaperone binding / protein stabilization / ubiquitin protein ligase binding / protein kinase binding / perinuclear region of cytoplasm / mitochondrion / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Hatta, R. / Hayashi, F. / Yoshida, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange Authors: Arakawa, A. / Handa, N. / Ohsawa, N. / Shida, M. / Kigawa, T. / Hayashi, F. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 544.7 KB | Display | ![]() |
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PDB format | ![]() | 458 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 343.1 KB | Display | ![]() |
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Full document | ![]() | 475.8 KB | Display | |
Data in XML | ![]() | 30.3 KB | Display | |
Data in CIF | ![]() | 46.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ugoC ![]() 1uk5C ![]() 3a8yC C: citing same article ( |
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Similar structure data | |
Other databases |
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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: 9842.250 Da / Num. of mol.: 1 / Fragment: BAG domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 0.96mM 13C, 15N-labeled protein; 20mM d-Tris-HCl (pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 75mM GuOx; 90% H2O; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 345mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function, structures with the lowest energy, structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |