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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Cryo-EM structure of the SPATA5-SPATA5L1-CINP-C1orf109 complex | |||||||||
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![]() | ribosomal biogenesis / SPATA5 / ATPase complex / CYTOSOLIC PROTEIN | |||||||||
Function / homology | ![]() chromatin extrusion motor activity / ATP-dependent H2AZ histone chaperone activity / ATP-dependent H3-H4 histone complex chaperone activity / cohesin loader activity / preribosome binding / DNA clamp loader activity / non-chaperonin molecular chaperone ATPase / ribosomal large subunit biogenesis / brain development / spindle ...chromatin extrusion motor activity / ATP-dependent H2AZ histone chaperone activity / ATP-dependent H3-H4 histone complex chaperone activity / cohesin loader activity / preribosome binding / DNA clamp loader activity / non-chaperonin molecular chaperone ATPase / ribosomal large subunit biogenesis / brain development / spindle / spermatogenesis / cell differentiation / DNA replication / cell division / DNA repair / ATP hydrolysis activity / ATP binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.51 Å | |||||||||
![]() | Dai Y / Zhang Y / Gao N | |||||||||
Funding support | ![]()
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![]() | ![]() Title: cryo-EM structure of the SPATA5-SPATA5L1-CINP-C1orf109 complex Authors: Dai Y / Zhang Y / Gao N | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 31 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16 KB 16 KB | Display Display | ![]() |
Images | ![]() | 87.7 KB | ||
Filedesc metadata | ![]() | 6.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9lgoMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.092 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : The SPATA5 complex
Entire | Name: The SPATA5 complex |
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Components |
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-Supramolecule #1: The SPATA5 complex
Supramolecule | Name: The SPATA5 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: ATPase family gene 2 protein homolog A
Macromolecule | Name: ATPase family gene 2 protein homolog A / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: non-chaperonin molecular chaperone ATPase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 97.276453 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSSKKNRKRL NQSAENGSSL PSAASSCAEA RAPSAGSDFA ATSGTLTVTN LLEKVDDKIP KTFQNSLIHL GLNTMKSANI CIGRPVLLT SLNGKQEVYT AWPMAGFPGG KVGLSEMAQK NVGVRPGDAI QVQPLVGAVL QAEEMDVALS DKDMEINEEE L TGCILRKL ...String: MSSKKNRKRL NQSAENGSSL PSAASSCAEA RAPSAGSDFA ATSGTLTVTN LLEKVDDKIP KTFQNSLIHL GLNTMKSANI CIGRPVLLT SLNGKQEVYT AWPMAGFPGG KVGLSEMAQK NVGVRPGDAI QVQPLVGAVL QAEEMDVALS DKDMEINEEE L TGCILRKL DGKIVLPGNF LYCTFYGRPY KLQVLRVKGA DGMILGGPQS DSDTDAQRMA FEQSSMETSS LELSLQLSQL DL EDTQIPT SRSTPYKPID DRITNKASDV LLDVTQSPGD GSGLMLEEVT GLKCNFESAR EGNEQLTEEE RLLKFSIGAK CNT DTFYFI SSTTRVNFTE IDKNSKEQDN QFKVTYDMIG GLSSQLKAIR EIIELPLKQP ELFKSYGIPA PRGVLLYGPP GTGK TMIAR AVANEVGAYV SVINGPEIIS KFYGETEAKL RQIFAEATLR HPSIIFIDQL DALCPKREGA QNEVEKRVVA SLLTL MDGI GSEVSEGQVL VLGATNRPHA LDAALRRPGR FDKEIEIGVP NAQDRLDILQ KLLRRVPHLL TEAELLQLAN SAHGYV GAD LKVLCNEAGL CALRRILKKQ PNLPDVKVAG LVKITLKDFL QAMNDIRPSA MREIAIDVPN VSWSDIGGLE SIKLKLE QA VEWPLKHPES FIRMGIQPPK GVLLYGPPGC SKTMIAKALA NESGLNFLAI KGPELMNKYV GESERAVRET FRKARAVA P SIIFFDQLDA LAVERGSSLG AGNVADRVLA QLLTEMDGIE QLKDVTILAA TNRPDRIDKA LMRPGRIDRI IYVPLPDAA TRREIFKLQF HSMPVSNEVD LDELILQTDA YSGAEIVAVC REAALLALEE DIQANLIMKR HFTQALSTVT PRIPESLRRF YEDYQE UniProtKB: ATPase family gene 2 protein homolog A |
-Macromolecule #2: Cyclin-dependent kinase 2-interacting protein
Macromolecule | Name: Cyclin-dependent kinase 2-interacting protein / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.42109 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLL NKDKIELDSS SPASKENEEK VCLEYNEELE KLCEELQATL DGLTKIQVKM EKLSSTTKGI CELENYHYGE E SKRPPLFH ...String: MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLL NKDKIELDSS SPASKENEEK VCLEYNEELE KLCEELQATL DGLTKIQVKM EKLSSTTKGI CELENYHYGE E SKRPPLFH TWPTTHFYEV SHKLLEMYRK ELLLKRTVAK ELAHTGDPDL TLSYLSMWLH QPYVESDSRL HLESMLLETG HR AL UniProtKB: Cyclin-dependent kinase 2-interacting protein |
-Macromolecule #3: cDNA FLJ55172
Macromolecule | Name: cDNA FLJ55172 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 31.59227 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MYPYDVPDYA MSEKRRRLDA RNPLKQETAL SRLPFPRGNQ GLLQKAEAGR ARWLTPVIPA LWKTEAGGSP EKMTQDRPLL AVQEALKKC FPVVEEQQGL WQSALRDCQP LLSSLSNLAE QLQAAQNLRF EDVPALRAFP DLKERLRRKQ LVAGDIVLDK L GERLAILL ...String: MYPYDVPDYA MSEKRRRLDA RNPLKQETAL SRLPFPRGNQ GLLQKAEAGR ARWLTPVIPA LWKTEAGGSP EKMTQDRPLL AVQEALKKC FPVVEEQQGL WQSALRDCQP LLSSLSNLAE QLQAAQNLRF EDVPALRAFP DLKERLRRKQ LVAGDIVLDK L GERLAILL KVRDMVSSHV ERVFQIYEQH ADTVGIDAVL QPSAVSPSVA DMLEWLQDIE RHYRKSYLKR KYLLSSIQWG DL ANIQALP KAWDRISKDE HQDLVQDILL NVSFFLEE UniProtKB: cDNA FLJ55172 |
-Macromolecule #4: ATPase family gene 2 protein homolog B
Macromolecule | Name: ATPase family gene 2 protein homolog B / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO / EC number: non-chaperonin molecular chaperone ATPase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 80.409742 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAPDSDPFPE GPLLKLLPLD ARDRGTQRCR LGPAALHALG ARLGSAVKIS LPDGGSCLCT AWPRRDGADG FVQLDPLCAS PGAAVGASR SRRSLSLNRL LLVPCPPLRR VAVWPVLRER AGAPGARNTA AVLEAAQELL RNRPISLGHV VVAPPGAPGL V AALHIVGG ...String: MAPDSDPFPE GPLLKLLPLD ARDRGTQRCR LGPAALHALG ARLGSAVKIS LPDGGSCLCT AWPRRDGADG FVQLDPLCAS PGAAVGASR SRRSLSLNRL LLVPCPPLRR VAVWPVLRER AGAPGARNTA AVLEAAQELL RNRPISLGHV VVAPPGAPGL V AALHIVGG TPSPDPAGLV TPRTRVSLGG EPPSEAQPQP EVPLGGLSEA ADSLRELLRL PLRYPRALTA LGLAVPRGVL LA GPPGVGK TQLVRAVARE AGAELLAVSA PALQGSRPGE TEENVRRVFQ RARELASRGP SLLFLDEMDA LCPQRGSRAP ESR VVAQVL TLLDGASGDR EVVVVGATNR PDALDPALRR PGRFDREVVI GTPTLKQRKE ILQVITSKMP ISSHVDLGLL AEMT VGYVG ADLTALCREA AMHALLHSEK NQDNPVIDEI DFLEAFKNIQ PSSFRSVIGL MDIKPVDWEE IGGLEDVKLK LKQSI EWPL KFPWEFVRMG LTQPKGVLLY GPPGCAKTTL VRALATSCHC SFVSVSGADL FSPFVGDSEK VLSQIFRQAR ASTPAI LFL DEIDSILGAR SASKTGCDVQ ERVLSVLLNE LDGVGLKTIE RRGSKSSQQE FQEVFNRSVM IIAATNRPDV LDTALLR PG RLDKIIYIPP PDHKGRLSIL KVCTKTMPIG PDVSLENLAA ETCFFSGADL RNLCTEAALL ALQENGLDAT TVKQEHFL K SLKTVKPSLS CKDLALYENL FKKEGFSN UniProtKB: ATPase family gene 2 protein homolog B |
-Macromolecule #5: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 8 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Macromolecule #6: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 1 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1.2 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.51 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 194789 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |