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Open data
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Basic information
Entry | Database: PDB / ID: 8k2t | ||||||
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Title | Solution structure of full-length HtpG in complex with D131D | ||||||
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![]() | CHAPERONE / HtpG / E coli Hsp90 | ||||||
Function / homology | ![]() endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters / micrococcal nuclease / ATP-dependent protein folding chaperone / unfolded protein binding / response to heat / nucleic acid binding / DNA damage response / perinuclear region of cytoplasm / ATP hydrolysis activity / extracellular region ...endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters / micrococcal nuclease / ATP-dependent protein folding chaperone / unfolded protein binding / response to heat / nucleic acid binding / DNA damage response / perinuclear region of cytoplasm / ATP hydrolysis activity / extracellular region / ATP binding / membrane / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Qu, X. / Huang, C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for the dynamic chaperoning of disordered clients by Hsp90. Authors: Qu, X. / Zhao, S. / Wan, C. / Zhu, L. / Ji, T. / Rossi, P. / Wang, J. / Kalodimos, C.G. / Wang, C. / Xu, W. / Huang, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 9.3 MB | Display | ![]() |
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PDB format | ![]() | 7.9 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 8k2rC ![]() 8k2sC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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: 71519.422 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | | Mass: 15033.458 Da / Num. of mol.: 1 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 | Type: solution Contents: 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90(HtpG M domain), 500 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG M ...Contents: 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90(HtpG M domain), 500 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG M domian), 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90(HtpG N domain), 500 uM [U-100% 13C; U-100% 15N] Disordered protein(D131D), 500 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG N domain), 600 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG C domain), 500 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG-D131D), 500 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG M-D131D N), 500 uM [U-2H, 15N; Ala- 13CH3; Met- 13CH3; Ile-d1- 13CH3; Leu, Val- 13CH3/ 13CH3; Thr- 13CH3] Heat shock protein 90(HtpG M-D131D C), 93% H2O/7% D2O Label: 13C_samples / Solvent system: 93% H2O/7% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 150 mM / Label: condition1 / pH: 7 / Pressure: 1 Pa / Temperature: 310 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 3 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |