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Open data
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Basic information
Entry | Database: PDB / ID: 9c9z | ||||||
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Title | S.c INO80 in complex with Xenopus 0/80 nucleosome, INO80 Core | ||||||
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![]() | DNA BINDING PROTEIN / Chromatin Remodeler / nucleosome | ||||||
Function / homology | ![]() TTT Hsp90 cochaperone complex / R2TP complex / regulation of TOR signaling / Swr1 complex / telomere maintenance via recombination / Ino80 complex / ATP-dependent chromatin remodeler activity / box C/D snoRNP assembly / regulation of metabolic process / 3'-5' DNA helicase activity ...TTT Hsp90 cochaperone complex / R2TP complex / regulation of TOR signaling / Swr1 complex / telomere maintenance via recombination / Ino80 complex / ATP-dependent chromatin remodeler activity / box C/D snoRNP assembly / regulation of metabolic process / 3'-5' DNA helicase activity / cellular response to stress / NuA4 histone acetyltransferase complex / chromosome, centromeric region / subtelomeric heterochromatin formation / enzyme regulator activity / DNA helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / rRNA processing / 5'-3' DNA helicase activity / DNA helicase / histone binding / single-stranded 3'-5' DNA helicase activity / double-stranded DNA helicase activity / forked DNA-dependent helicase activity / four-way junction helicase activity / transcription by RNA polymerase II / chromosome, telomeric region / protein stabilization / chromatin remodeling / DNA repair / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.55 Å | ||||||
![]() | Wu, H. / Kaur, U. / Narlikar, G.J. / Cheng, Y.F. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Autoinhibition imposed by a large conformational switch of INO80 regulates nucleosome positioning Authors: Kaur, U. / Wu, H. / Cheng, Y. / Narlikar, G.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 746.1 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 100.2 KB | Display | |
Data in CIF | ![]() | 154.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 45377MC ![]() 9c9gC ![]() 9c9sC ![]() 9c9tC ![]() 9c9xC ![]() 9canC ![]() 9catC ![]() 9cauC ![]() 9cb7C ![]() 9ccdC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Chromatin-remodeling ... , 2 types, 2 molecules QS
#1: Protein | Mass: 171693.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P53115, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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#3: Protein | Mass: 18564.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein , 2 types, 2 molecules RZ
#2: Protein | Mass: 87682.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#6: Protein | Mass: 36210.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-RuvB-like protein ... , 2 types, 6 molecules TVXUWY
#4: Protein | Mass: 50516.941 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 50539.367 Da / Num. of mol.: 3 / Fragment: residues 1-460 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Non-polymers , 1 types, 6 molecules 
#7: Chemical | ChemComp-ADP / |
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-Details
Has ligand of interest | Y |
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Has protein modification | N |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: CELL / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: S.c INO80 in complex with Xenopus 0/80 nucleosome, INO80 Core Type: COMPLEX / Entity ID: #1-#6 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: OTHER |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 47.7 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
3D reconstruction | Resolution: 2.55 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 109876 / Symmetry type: POINT |