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- PDB-8k2r: The structure of HtpG M domain in complex with unstructured D131D... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8k2r | ||||||
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Title | The structure of HtpG M domain in complex with unstructured D131D binding site b | ||||||
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![]() | CHAPERONE / 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 / molecular dynamics | ||||||
![]() | 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. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.4 MB | Display | ![]() |
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PDB format | ![]() | 2 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 8k2sC ![]() 8k2tC 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: 31353.383 Da / Num. of mol.: 1 / Fragment: Heat shock protein 90 (Hsp90) M domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 8795.115 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-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-100% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-10% 13C; U-99% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90 (Hsp90) M ...Contents: 500 uM [U-100% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-10% 13C; U-99% 15N] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-13C; U-15N; U-2H] Heat shock protein 90 (Hsp90) M domain, 500 uM [U-100% 13C; U-100% 15N] Disordered protein (D131D), 93% H2O/7% D2O Label: 13CH3_sample / Solvent system: 93% H2O/7% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 150 mM / Label: condition_1 / 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: 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 |