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Open data
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Basic information
Entry | Database: PDB / ID: 8xvg | ||||||
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Title | Structure of human NuA4/TIP60 complex | ||||||
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![]() | TRANSCRIPTION / Remodeler / Histone Acetyltransferase Complex / NuA4 / TIP60 | ||||||
Function / homology | ![]() ATP-dependent H2AZ histone chaperone activity / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / histone chaperone activity / sperm DNA condensation / establishment of protein localization to chromatin / npBAF complex / brahma complex ...ATP-dependent H2AZ histone chaperone activity / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / histone chaperone activity / sperm DNA condensation / establishment of protein localization to chromatin / npBAF complex / brahma complex / R2TP complex / transcription factor TFTC complex / dynein axonemal particle / chromatin-protein adaptor activity / RPAP3/R2TP/prefoldin-like complex / GBAF complex / protein antigen binding / Swr1 complex / regulation of G0 to G1 transition / neural retina development / positive regulation of telomerase RNA localization to Cajal body / regulation of double-strand break repair / regulation of nucleotide-excision repair / Ino80 complex / RSC-type complex / blastocyst formation / Regulation of MITF-M-dependent genes involved in pigmentation / enzyme-substrate adaptor activity / protein folding chaperone complex / regulation of mitotic metaphase/anaphase transition / SWI/SNF complex / box C/D snoRNP assembly / ATP-dependent chromatin remodeler activity / SAGA complex / positive regulation of double-strand break repair / positive regulation of T cell differentiation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / negative regulation of gene expression, epigenetic / spinal cord development / regulation of chromosome organization / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / Transcriptional Regulation by E2F6 / regulation of DNA replication / regulation of G1/S transition of mitotic cell cycle / regulation of RNA splicing / somatic stem cell population maintenance / TFIID-class transcription factor complex binding / negative regulation of cell differentiation / regulation of embryonic development / MLL1 complex / Telomere Extension By Telomerase / spermatid development / positive regulation of double-strand break repair via homologous recombination / RNA polymerase II core promoter sequence-specific DNA binding / positive regulation of myoblast differentiation / regulation of DNA repair / histone acetyltransferase activity / Deposition of new CENPA-containing nucleosomes at the centromere / TBP-class protein binding / DNA helicase activity / positive regulation of DNA repair / telomere maintenance / transcription initiation-coupled chromatin remodeling / replication fork / helicase activity / cellular response to estradiol stimulus / positive regulation of cell differentiation / transcription coregulator activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Formation of the beta-catenin:TCF transactivating complex / double-strand break repair via homologous recombination / DNA Damage Recognition in GG-NER / negative regulation of canonical Wnt signaling pathway / euchromatin / DNA Damage/Telomere Stress Induced Senescence / chromatin DNA binding / kinetochore / ADP binding / RMTs methylate histone arginines / nuclear matrix / beta-catenin binding / positive regulation of protein import into nucleus / transcription corepressor activity / UCH proteinases / cellular response to UV / nucleosome / unfolded protein binding / positive regulation of canonical Wnt signaling pathway / protein folding / chromatin organization / nervous system development / site of double-strand break / HATs acetylate histones / histone binding / ATPase binding / spermatogenesis / nuclear membrane / DNA helicase Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 9.4 Å | ||||||
![]() | Chen, K. / Wang, L. / Yu, Z. / Yu, J. / Ren, Y. / Wang, Q. / Xu, Y. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the human TIP60 complex Authors: Chen, K. / Wang, L. / Yu, Z. / Yu, J. / Ren, Y. / Wang, Q. / Xu, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.1 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 38703MC ![]() 8xvtC ![]() 8xvvC 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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Components
-Isoform 2 of ... , 3 types, 3 molecules LHM
#1: Protein | Mass: 434949.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#5: Protein | Mass: 340198.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q96L91, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
#8: Protein | Mass: 90988.273 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein , 6 types, 11 molecules ACEBDFGIJKN
#2: Protein | Mass: 50296.914 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Protein | Mass: 51222.465 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #4: Protein | | Mass: 53090.699 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #6: Protein | Mass: 47509.812 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #7: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #9: Protein | | Mass: 40658.363 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 2 types, 10 molecules ![](data/chem/img/IHP.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/ADP.gif)
#10: Chemical | ChemComp-IHP / |
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#11: Chemical | ChemComp-ADP / |
-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
Component | Name: Structure of human NuA4/TIP60 complex / Type: COMPLEX / Entity ID: #2-#7, #1, #8-#9 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.4 |
Specimen | 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 / Nominal defocus max: 2800 nm / Nominal defocus min: 1500 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 9.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 20275 / Symmetry type: POINT |