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- EMDB-38718: The core subcomplex of human NuA4/TIP60 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-38718
TitleThe core subcomplex of human NuA4/TIP60 complex
Map dataThe core subcomplex of human TIP60 complex
Sample
  • Complex: The core subcomplex of human NuA4/TIP60 complex
    • Protein or peptide: RuvB-like 1
    • Protein or peptide: RuvB-like 2
    • Protein or peptide: DNA methyltransferase 1-associated protein 1
    • Protein or peptide: Isoform 2 of E1A-binding protein p400
    • Protein or peptide: Actin-like protein 6A
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Isoform 2 of Enhancer of polycomb homolog 1
    • Protein or peptide: Vacuolar protein sorting-associated protein 72 homolog
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsRemodeler / Histone Acetyltransferase Complex / NuA4 / TIP60 / TRANSCRIPTION
Function / homology
Function and homology information


ATP-dependent H2AZ histone chaperone activity / : / : / vascular associated smooth muscle cell differentiation / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage ...ATP-dependent H2AZ histone chaperone activity / : / : / vascular associated smooth muscle cell differentiation / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / regulation of transepithelial transport / histone chaperone activity / establishment of protein localization to chromatin / morphogenesis of a polarized epithelium / bBAF complex / postsynaptic actin cytoskeleton organization / protein localization to adherens junction / postsynaptic actin cytoskeleton / R2TP complex / npBAF complex / dynein axonemal particle / Tat protein binding / structural constituent of postsynaptic actin cytoskeleton / brahma complex / nBAF complex / protein antigen binding / RPAP3/R2TP/prefoldin-like complex / Swr1 complex / GBAF complex / neural retina development / dense body / regulation of G0 to G1 transition / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / apical protein localization / regulation of double-strand break repair / positive regulation of telomerase RNA localization to Cajal body / negative regulation of G0 to G1 transition / Ino80 complex / regulation of nucleotide-excision repair / adherens junction assembly / Prefoldin mediated transfer of substrate to CCT/TriC / blastocyst formation / RHOF GTPase cycle / RSC-type complex / Adherens junctions interactions / tight junction / protein folding chaperone complex / Sensory processing of sound by outer hair cells of the cochlea / regulation of norepinephrine uptake / Interaction between L1 and Ankyrins / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / regulation of growth / ATP-dependent chromatin remodeler activity / box C/D snoRNP assembly / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / positive regulation of T cell differentiation / apical junction complex / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / establishment or maintenance of cell polarity / negative regulation of gene expression, epigenetic / regulation of cyclin-dependent protein serine/threonine kinase activity / spinal cord development / regulation of chromosome organization / cortical cytoskeleton / maintenance of blood-brain barrier / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / 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 / Recycling pathway of L1 / kinesin binding / brush border / somatic stem cell population maintenance / calyx of Held / negative regulation of cell differentiation / TFIID-class transcription factor complex binding / regulation of embryonic development / MLL1 complex / Telomere Extension By Telomerase / positive regulation of double-strand break repair via homologous recombination / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / RNA polymerase II core promoter sequence-specific DNA binding / positive regulation of myoblast differentiation / regulation of DNA repair / DNA helicase activity / Deposition of new CENPA-containing nucleosomes at the centromere / transcription initiation-coupled chromatin remodeling / EPHB-mediated forward signaling
Similarity search - Function
Enhancer of polycomb, C-terminal / Enhancer of Polycomb C-terminus / E1A-binding protein p400, N-terminal / E1A-binding protein p400, N-terminal / Vps72/YL1, N-terminal / DNA methyltransferase 1-associated 1 / Vps72/YL1 family / DNA methyltransferase 1-associated protein 1 (DMAP1) / YL1 nuclear protein / SWR1-complex protein 4/DNA methyltransferase 1-associated protein 1 ...Enhancer of polycomb, C-terminal / Enhancer of Polycomb C-terminus / E1A-binding protein p400, N-terminal / E1A-binding protein p400, N-terminal / Vps72/YL1, N-terminal / DNA methyltransferase 1-associated 1 / Vps72/YL1 family / DNA methyltransferase 1-associated protein 1 (DMAP1) / YL1 nuclear protein / SWR1-complex protein 4/DNA methyltransferase 1-associated protein 1 / DAMP1, SANT/Myb-like domain / SANT/Myb-like domain of DAMP1 / Enhancer of polycomb protein / Vps72/YL1, C-terminal / YL1 nuclear protein C-terminal domain / YL1 nuclear protein C-terminal domain / Myb-like domain profile. / domain in helicases and associated with SANT domains / RuvB-like / RuvB-like, AAA-lid domain / RuvBL1/2, DNA/RNA binding domain / TIP49 P-loop domain / TIP49 AAA-lid domain / TIP49, P-loop domain / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Enhancer of polycomb-like, N-terminal / Enhancer of polycomb-like / SANT/Myb domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Helicase conserved C-terminal domain / ATPase, nucleotide binding domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Actin-like protein 6A / Actin, cytoplasmic 1 / Vacuolar protein sorting-associated protein 72 homolog / E1A-binding protein p400 / Enhancer of polycomb homolog 1 / DNA methyltransferase 1-associated protein 1 / RuvB-like 2 / RuvB-like 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsChen K / Wang L / Yu Z / Yu J / Ren Y / Wang Q / Xu Y
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Nat Commun / Year: 2024
Title: Structure of the human TIP60 complex
Authors: Chen K / Wang L / Yu Z / Yu J / Ren Y / Wang Q / Xu Y
History
DepositionJan 15, 2024-
Header (metadata) releaseJul 24, 2024-
Map releaseJul 24, 2024-
UpdateJul 24, 2024-
Current statusJul 24, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_38718.png

Downloads & links

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Map

FileDownload / File: emd_38718.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe core subcomplex of human TIP60 complex
Projections & slices

Image control

Size
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.33 Å/pix.
x 300 pix.
= 400.2 Å		1.33 Å/pix.
x 300 pix.
= 400.2 Å		1.33 Å/pix.
x 300 pix.
= 400.2 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.334 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.024
Minimum - Maximum-0.12466709 - 0.25158393
Average (Standard dev.)0.0003176818 (±0.007099864)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 400.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: The actin-related module of human TIP60 complex

Fileemd_38718_additional_1.map
AnnotationThe actin-related module of human TIP60 complex
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: Human TIP60 core subcomplex half map2

Fileemd_38718_half_map_1.map
AnnotationHuman TIP60 core subcomplex half map2
Projections & Slices
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Histogram (log scale)

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Half map: Human TIP60 core subcomplex half map1

Fileemd_38718_half_map_2.map
AnnotationHuman TIP60 core subcomplex half map1
Projections & Slices
AxesZYX

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Sample components

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Entire : The core subcomplex of human NuA4/TIP60 complex

EntireName: The core subcomplex of human NuA4/TIP60 complex
Components
  • Complex: The core subcomplex of human NuA4/TIP60 complex
    • Protein or peptide: RuvB-like 1
    • Protein or peptide: RuvB-like 2
    • Protein or peptide: DNA methyltransferase 1-associated protein 1
    • Protein or peptide: Isoform 2 of E1A-binding protein p400
    • Protein or peptide: Actin-like protein 6A
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Isoform 2 of Enhancer of polycomb homolog 1
    • Protein or peptide: Vacuolar protein sorting-associated protein 72 homolog
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: The core subcomplex of human NuA4/TIP60 complex

SupramoleculeName: The core subcomplex of human NuA4/TIP60 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: RuvB-like 1

MacromoleculeName: RuvB-like 1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.296914 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGS KVPFCPMVGS EVYSTEIKKT EVLMENFRRA IGLRIKETKE VYEGEVTELT PCETENPMGG YGKTISHVII G LKTAKGTK ...String:
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGS KVPFCPMVGS EVYSTEIKKT EVLMENFRRA IGLRIKETKE VYEGEVTELT PCETENPMGG YGKTISHVII G LKTAKGTK QLKLDPSIFE SLQKERVEAG DVIYIEANSG AVKRQGRCDT YATEFDLEAE EYVPLPKGDV HKKKEIIQDV TL HDLDVAN ARPQGGQDIL SMMGQLMKPK KTEITDKLRG EINKVVNKYI DQGIAELVPG VLFVDEVHML DIECFTYLHR ALE SSIAPI VIFASNRGNC VIRGTEDITS PHGIPLDLLD RVMIIRTMLY TPQEMKQIIK IRAQTEGINI SEEALNHLGE IGTK TTLRY SVQLLTPANL LAKINGKDSI EKEHVEEISE LFYDAKSSAK ILADQQDKYM K

UniProtKB: RuvB-like 1

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Macromolecule #2: RuvB-like 2

MacromoleculeName: RuvB-like 2 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.222465 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMG MAQALGPDTP FTAIAGSEIF SLEMSKTEAL TQAFRRSIGV RIKEETEIIE GEVVEIQIDR PATGTGSKVG K LTLKTTEM ...String:
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMG MAQALGPDTP FTAIAGSEIF SLEMSKTEAL TQAFRRSIGV RIKEETEIIE GEVVEIQIDR PATGTGSKVG K LTLKTTEM ETIYDLGTKM IESLTKDKVQ AGDVITIDKA TGKISKLGRS FTRARDYDAM GSQTKFVQCP DGELQKRKEV VH TVSLHEI DVINSRTQGF LALFSGDTGE IKSEVREQIN AKVAEWREEG KAEIIPGVLF IDEVHMLDIE SFSFLNRALE SDM APVLIM ATNRGITRIR GTSYQSPHGI PIDLLDRLLI VSTTPYSEKD TKQILRIRCE EEDVEMSEDA YTVLTRIGLE TSLR YAIQL ITAASLVCRK RKGTEVQVDD IKRVYSLFLD ESRSTQYMKE YQDAFLFNEL KGETMDTS

UniProtKB: RuvB-like 2

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Macromolecule #3: DNA methyltransferase 1-associated protein 1

MacromoleculeName: DNA methyltransferase 1-associated protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 53.090699 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL LYSDKKDAPP LLPSDTGQGY RTVKAKLGS KKVRPWKWMP FTNPARKDGA MFFHWRRAAE EGKDYPFARF NKTVQVPVYS EQEYQLYLHD DAWTKAETDH L FDLSRRFD ...String:
MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL LYSDKKDAPP LLPSDTGQGY RTVKAKLGS KKVRPWKWMP FTNPARKDGA MFFHWRRAAE EGKDYPFARF NKTVQVPVYS EQEYQLYLHD DAWTKAETDH L FDLSRRFD LRFVVIHDRY DHQQFKKRSV EDLKERYYHI CAKLANVRAV PGTDLKIPVF DAGHERRRKE QLERLYNRTP EQ VAEEEYL LQELRKIEAR KKEREKRSQD LQKLITAADT TAEQRRTERK APKKKLPQKK EAEKPAVPET AGIKFPDFKS AGV TLRSQR MKLPSSVGQK KIKALEQMLL ELGVELSPTP TEELVHMFNE LRSDLVLLYE LKQACANCEY ELQMLRHRHE ALAR AGVLG GPATPASGPG PASAEPAVTE PGLGPDPKDT IIDVVGAPLT PNSRKRRESA SSSSSVKKAK KP

UniProtKB: DNA methyltransferase 1-associated protein 1

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Macromolecule #4: Isoform 2 of E1A-binding protein p400

MacromoleculeName: Isoform 2 of E1A-binding protein p400 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 340.198062 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQI TLAPLPLPSP TSPGFQFSAQ PRRFEHGSPS YIQVTSPLSQ QVQTQSPTQP SPGPGQALQN VRAGAPGPGL G LCSSSPTG ...String:
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQI TLAPLPLPSP TSPGFQFSAQ PRRFEHGSPS YIQVTSPLSQ QVQTQSPTQP SPGPGQALQN VRAGAPGPGL G LCSSSPTG GFVDASVLVR QISLSPSSGG HFVFQDGSGL TQIAQGAQVQ LQHPGTPITV RERRPSQPHT QSGGTIHHLG PQ SPAAAGG AGLQPLASPS HITTANLPPQ ISSIIQGQLV QQQQVLQGPP LPRPLGFERT PGVLLPGAGG AAGFGMTSPP PPT SPSRTA VPPGLSSLPL TSVGNTGMKK VPKKLEEIPP ASPEMAQMRK QCLDYHYQEM QALKEVFKEY LIELFFLQHF QGNM MDFLA FKKKHYAPLQ AYLRQNDLDI EEEEEEEEEE EEKSEVINDE QQALAGSLVA GAGSTVETDL FKRQQAMPST GMAEQ SKRP RLEVGHQGVV FQHPGADAGV PLQQLMPTAQ GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGR LPP AGVPTAALSS ALQFAQQPQV VEAQTQLQIP VKTQQPNVPI PAPPSSQLPI PPSQPAQLAL HVPTPGKVQV QASQLSS LP QMVASTRLPV DPAPPCPRPL PTSSTSSLAP VSGSGPGPSP ARSSPVNRPS SATNKALSPV TSRTPGVVAS APTKPQSP A QNATSSQDSS QDTLTEQITL ENQVHQRIAE LRKAGLWSQR RLPKLQEAPR PKSHWDYLLE EMQWMATDFA QERRWKVAA AKKLVRTVVR HHEEKQLREE RGKKEEQSRL RRIAASTARE IECFWSNIEQ VVEIKLRVEL EEKRKKALNL QKVSRRGKEL RPKGFDALQ ESSLDSGMSG RKRKASISLT DDEVDDEEET IEEEEANEGV VDHQTELSNL AKEAELPLLD LMKLYEGAFL P SSQWPRPK PDGEDTSGEE DADDCPGDRE SRKDLVLIDS LFIMDQFKAA ERMNIGKPNA KDIADVTAVA EAILPKGSAR VT TSVKFNA PSLLYGALRD YQKIGLDWLA KLYRKNLNGI LADEAGLGKT VQIIAFFAHL ACNEGNWGPH LVVVRSCNIL KWE LELKRW CPGLKILSYI GSHRELKAKR QEWAEPNSFH VCITSYTQFF RGLTAFTRVR WKCLVIDEMQ RVKGMTERHW EAVF TLQSQ QRLLLIDSPL HNTFLELWTM VHFLVPGISR PYLSSPLRAP SEESQDYYHK VVIRLHRVTQ PFILRRTKRD VEKQL TKKY EHVLKCRLSN RQKALYEDVI LQPGTQEALK SGHFVNVLSI LVRLQRICNH PGLVEPRHPG SSYVAGPLEY PSASLI LKA LERDFWKEAD LSMFDLIGLE NKITRHEAEL LSKKKIPRKL MEEISTSAAP AARPAAAKLK ASRLFQPVQY GQKPEGR TV AFPSTHPPRT AAPTTASAAP QGPLRGRPPI ATFSANPEAK AAAAPFQTSQ ASASAPRHQP ASASSTAASP AHPAKLRA Q TTAQASTPGQ PPPQPQAPSH AAGQSALPQR LVLPSQAQAR LPSGEVVKIA QLASITGPQS RVAQPETPVT LQFQGSKFT LSHSQLRQLT AGQPLQLQGS VLQIVSAPGQ PYLRAPGPVV MQTVSQAGAV HGALGSKPPA GGPSPAPLTP QVGVPGRVAV NALAVGEPG TASKPASPIG GPTQEEKTRL LKERLDQIYL VNERRCSQAP VYGRDLLRIC ALPSHGRVQW RGSLDGRRGK E AGPAHSYT SSSESPSELM LTLCRCGESL QDVIDRVAFV IPPVVAAPPS LRVPRPPPLY SHRMRILRQG LREHAAPYFQ QL RQTTAPR LLQFPELRLV QFDSGKLEAL AILLQKLKSE GRRVLILSQM ILMLDILEMF LNFHYLTYVR IDENASSEQR QEL MRSFNR DRRIFCAILS THSRTTGINL VEADTVVFYD NDLNPVMDAK AQEWCDRIGR CKDIHIYRLV SGNSIEEKLL KNGT KDLIR EVAAQGNDYS MAFLTQRTIQ ELFEVYSPMD DAGFPVKAEE FVVLSQEPSV TETIAPKIAR PFIEALKSIE YLEED AQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE ELADFMEQLT PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAW EFW NLKTLQEREA RLRLEQEEAE LLTYTREDAY SMEYVYEDVD GQTEVMPLWT PPTPPQDDSD IYLDSVMCLM YEATPIP EA KLPPVYVRKE RKRHKTDPSA AGRKKKQRHG EAVVPPRSLF DRATPGLLKI RREGKEQKKN ILLKQQVPFA KPLPTFAK P TAEPGQDNPE WLISEDWALL QAVKQLLELP LNLTIVSPAH TPNWDLVSDV VNSCSRIYRS SKQCRNRYEN VIIPREEGK SKNNRPLRTS QIYAQDENAT HTQLYTSHFD LMKMTAGKRS PPIKPLLGMN PFQKNPKHAS VLAESGINYD KPLPPIQVAS LRAERIAKE KKALADQQKA QQPAVAQPPP PQPQPPPPPQ QPPPPLPQPQ AAGSQPPAGP PAVQPQPQPQ PQTQPQPVQA P AKAQPAIT TGGSAAVLAG TIKTSVTGTS MPTGAVSGNV IVNTIAGVPA ATFQSINKRL ASPVAPGALT TPGGSAPAQV VH TQPPPRA VGSPATATPD LVSMATTQGV RAVTSVTASA VVTTNLTPVQ TPARSLVPQV SQATGVQLPG KTITPAHFQL LRQ QQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQTTTTSQVQ VPQIQGQAQS PAQIKAVGKL TPEHLIKMQK QKLQMPPQPP PPQA QSAPP QPTAQVQVQT SQPPQQQSPQ LTTVTAPRPG ALLTGTTVAN LQVARLTRVP TSQLQAQGQM QTQAPQPAQV ALAKP PVVS VPAAVVSSPG VTTLPMNVAG ISVAIGQPQK AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKIT AQQ ITTPGAQQKV AYAAQPALKT QFLTTPISQA QKLAGAQQVQ TQIQVAKLPQ VVQQQTPVAS IQQVASASQQ ASPQTVA LT QATAAGQQVQ MIPAVTATAQ VVQQKLIQQQ VVTTASAPLQ TPGAPNPAQV PASSDSPSQQ PKLQMRVPAV RLKTPTKP P CQ

UniProtKB: E1A-binding protein p400

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Macromolecule #5: Actin-like protein 6A

MacromoleculeName: Actin-like protein 6A / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 47.509812 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLK NGMVEDWDSF QAILDHTYKM HVKSEASLHP VLMSEAPWNT RAKREKLTEL MFEHYNIPAF FLCKTAVLTA F ANGRSTGL ...String:
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLK NGMVEDWDSF QAILDHTYKM HVKSEASLHP VLMSEAPWNT RAKREKLTEL MFEHYNIPAF FLCKTAVLTA F ANGRSTGL ILDSGATHTT AIPVHDGYVL QQGIVKSPLA GDFITMQCRE LFQEMNIELV PPYMIASKEA VREGSPANWK RK EKLPQVT RSWHNYMCNC VIQDFQASVL QVSDSTYDEQ VAAQMPTVHY EFPNGYNCDF GAERLKIPEG LFDPSNVKGL SGN TMLGVS HVVTTSVGMC DIDIRPGLYG SVIVAGGNTL IQSFTDRLNR ELSQKTPPSM RLKLIANNTT VERRFSSWIG GSIL ASLGT FQQMWISKQE YEEGGKQCVE RKCP

UniProtKB: Actin-like protein 6A

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Macromolecule #6: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.78266 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #7: Isoform 2 of Enhancer of polycomb homolog 1

MacromoleculeName: Isoform 2 of Enhancer of polycomb homolog 1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 90.988273 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS AQQVYGEKRD NMVIPVPEAE SNIAYYESI YPGEFKMPKQ LIHIQPFSLD AEQPDYDLDS EDEVFVNKLK KKMDICPLQF EEMIDRLEKG SGQQPVSLQE A KLLLKEDD ...String:
MSKLSFRARA LDASKPLPVF RCEDLPDLHE YASINRAVPQ MPTGMEKEEE SEHHLQRAIS AQQVYGEKRD NMVIPVPEAE SNIAYYESI YPGEFKMPKQ LIHIQPFSLD AEQPDYDLDS EDEVFVNKLK KKMDICPLQF EEMIDRLEKG SGQQPVSLQE A KLLLKEDD ELIREVYEYW IKKRKNCRGP SLIPSVKQEK RDGSSTNDPY VAFRRRTEKM QTRKNRKNDE ASYEKMLKLR RD LSRAVTI LEMIKRREKS KRELLHLTLE IMEKRYNLGD YNGEIMSEVM AQRQPMKPTY AIPIIPITNS SQFKHQEAMD VKE FKVNKQ DKADLIRPKR KYEKKPKVLP SSAAATPQQT SPAALPVFNA KDLNQYDFPS SDEEPLSQVL SGSSEAEEDN DPDG PFAFR RKAGCQYYAP HLDQTGNWPW TSPKDGGLGD VRYRYCLTTL TVPQRCIGFA RRRVGRGGRV LLDRAHSDYD SVFHH LDLE MLSSPQHSPV NQFANTSETN TSDKSFSKDL SQILVNIKSC RWRHFRPRTP SLHDSDNDEL SCRKLYRSIN RTGTAQ PGT QTCSTSTQSK SSSGSAHFAF TAEQYQQHQQ QLALMQKQQL AQIQQQQANS NSSTNTSQGF VSKTLDSASA QFAASAL VT SEQLMGFKMK DDVVLGIGVN GVLPASGVYK GLHLSSTTPT ALVHTSPSTA GSALLQPSNI TQTSSSHSAL SHQVTAAN S ATTQVLIGNN IRLTVPSSVA TVNSIAPINA RHIPRTLSAV PSSALKLAAA ANCQVSKVPS SSSVDSVPRE NHESEKPAL NNIADNTVAM EVT

UniProtKB: Enhancer of polycomb homolog 1

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Macromolecule #8: Vacuolar protein sorting-associated protein 72 homolog

MacromoleculeName: Vacuolar protein sorting-associated protein 72 homolog
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.658363 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD FDIDEGDEPS SDGEAEEPRR KRRVVTKAY KEPLKSLRPR KVNTPAGSSQ KAREEKALLP LELQDDGSDS RKSMRQSTAE HTRQTFLRVQ ERQGQSRRRK G PHCERPLT ...String:
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD FDIDEGDEPS SDGEAEEPRR KRRVVTKAY KEPLKSLRPR KVNTPAGSSQ KAREEKALLP LELQDDGSDS RKSMRQSTAE HTRQTFLRVQ ERQGQSRRRK G PHCERPLT QEELLREAKI TEELNLRSLE TYERLEADKK KQVHKKRKCP GPIITYHSVT VPLVGEPGPK EENVDIEGLD PA PSVSALT PHAGTGPVNP PARCSRTFIT FSDDATFEEW FPQGRPPKVP VREVCPVTHR PALYRDPVTD IPYATARAFK IIR EAYKKY ITAHGLPPTA SALGPGPPPP EPLPGSGPRA LRQKIVIK

UniProtKB: Vacuolar protein sorting-associated protein 72 homolog

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Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 9 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6igm

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 701594
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6igm


Chain - Source name: PDB / Chain - Initial model type: experimental model
Output model

PDB-8xvt:
The core subcomplex of human NuA4/TIP60 complex

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