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Open data
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Basic information
Entry | Database: PDB / ID: 7egp | ||||||
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Title | The structure of SWI/SNF-nucleosome complex | ||||||
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![]() | DNA BINDING PROTEIN / Chromatin remodeler complex | ||||||
Function / homology | ![]() carbon catabolite activation of transcription from RNA polymerase II promoter / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / positive regulation of cell adhesion involved in single-species biofilm formation / positive regulation of mating type switching / positive regulation of pseudohyphal growth by positive regulation of transcription from RNA polymerase II promoter / positive regulation of invasive growth in response to glucose limitation / aggrephagy / Platelet degranulation ...carbon catabolite activation of transcription from RNA polymerase II promoter / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / positive regulation of cell adhesion involved in single-species biofilm formation / positive regulation of mating type switching / positive regulation of pseudohyphal growth by positive regulation of transcription from RNA polymerase II promoter / positive regulation of invasive growth in response to glucose limitation / aggrephagy / Platelet degranulation / rDNA binding / HDACs deacetylate histones / nucleosome disassembly / DNA strand invasion / RSC-type complex / ATP-dependent chromatin remodeler activity / SUMOylation of chromatin organization proteins / SWI/SNF complex / nuclear chromosome / NuA4 histone acetyltransferase complex / positive regulation of transcription by RNA polymerase I / anatomical structure morphogenesis / ATP-dependent activity, acting on DNA / nucleosomal DNA binding / helicase activity / maturation of LSU-rRNA / chromosome segregation / transcription elongation by RNA polymerase II / nucleotide-excision repair / transcription coregulator activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / double-strand break repair via homologous recombination / lysine-acetylated histone binding / chromatin DNA binding / DNA-templated DNA replication / structural constituent of chromatin / nucleosome / double-strand break repair / nucleosome assembly / chromatin organization / histone binding / RNA polymerase II-specific DNA-binding transcription factor binding / hydrolase activity / transcription cis-regulatory region binding / chromatin remodeling / protein heterodimerization activity / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / structural molecule activity / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / ATP binding / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() synthetic construct (others) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.9 Å | ||||||
![]() | Chen, Z.C. / Chen, K.J. / He, Z.Y. / Ye, Y.P. | ||||||
![]() | ![]() Title: Structure of the SWI/SNF complex bound to the nucleosome and insights into the functional modularity. Authors: Zhenyu He / Kangjing Chen / Youpi Ye / Zhucheng Chen / ![]() | ||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 822.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1014.5 KB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 139.8 KB | Display | |
Data in CIF | ![]() | 216.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 31137MC ![]() 7eg6C ![]() 7egmC C: citing same article ( M: map data used to model this data |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-SWI/SNF chromatin-remodeling complex subunit ... , 2 types, 2 molecules BC
#1: Protein | Mass: 124885.695 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SWI1, ADR6, GAM3, YPL016W, LPA1 Production host: ![]() References: UniProt: P09547 |
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#2: Protein | Mass: 103954.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SNF5, SWI10, TYE4, YBR289W, YBR2036 Production host: ![]() References: UniProt: P18480 |
-Protein , 9 types, 14 molecules DEJLMNOSPTQURV
#3: Protein | Mass: 94178.352 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SWI3, TYE2, YJL176C, J0495 Production host: ![]() References: UniProt: P32591 #6: Protein | | Mass: 71510.805 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SWP82, YFL049W Production host: ![]() References: UniProt: P43554 #8: Protein | | Mass: 17817.615 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: RTT102, YGR275W, G9378 Production host: ![]() References: UniProt: P53330 #9: Protein | | Mass: 53863.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: ARP7, SWP61, YPR034W, YP9367.14 Production host: ![]() References: UniProt: Q12406 #10: Protein | | Mass: 53131.930 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: ARP9, SWP59, YMR033W, YM9973.07 Production host: ![]() References: UniProt: Q05123 #11: Protein | Mass: 15289.904 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: P84233 #12: Protein | Mass: 11263.231 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: P62799 #13: Protein | Mass: 13978.241 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q6AZJ8 #14: Protein | Mass: 13524.752 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: P02281 |
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-Transcription regulatory protein ... , 3 types, 3 molecules HIA
#4: Protein | Mass: 63947.633 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SNF12, SWP73, YNR023W, N3224 Production host: ![]() References: UniProt: P53628 |
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#5: Protein | Mass: 37652.582 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SNF6, YHL025W Production host: ![]() References: UniProt: P18888 |
#7: Protein | Mass: 114311.914 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SNF2, GAM1, RIC1, SWI2, TYE3, YOR290C Production host: ![]() References: UniProt: P22082, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
-DNA chain , 2 types, 2 molecules WX
#15: DNA chain | Mass: 72380.109 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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#16: DNA chain | Mass: 72740.328 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 3 types, 3 molecules ![](data/chem/img/ADP.gif)
![](data/chem/img/BEF.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/BEF.gif)
![](data/chem/img/MG.gif)
#17: Chemical | ChemComp-ADP / |
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#18: Chemical | ChemComp-BEF / |
#19: Chemical | ChemComp-MG / |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||
Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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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 |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 6.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 229461 / Symmetry type: POINT |