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- EMDB-64663: Cryo-EM structure of cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(Z... -

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Entry
Database: EMDB / ID: EMD-64663
TitleCryo-EM structure of cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
Map data
Sample
  • Complex: Cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
    • Protein or peptide: Cullin-4A
    • Protein or peptide: DNA damage-binding protein 1
    • Protein or peptide: Protein cereblon
    • Protein or peptide: Ubiquitin-conjugating enzyme E2 D1
    • Protein or peptide: Zinc finger protein Aiolos
    • Protein or peptide: NEDD8
    • Protein or peptide: E3 ubiquitin-protein ligase RBX1, N-terminally processed
    • Protein or peptide: Ubiquitin
  • Ligand: Cemsidomide
  • Ligand: ZINC ION
KeywordsMolecular glue degrader / cemsidomide / CRL4 ubiquitin ligase / DDB1 / CRBN / Complex / LIGASE
Function / homology
Function and homology information


regulation of lymphocyte differentiation / regulation of B cell proliferation / regulation of B cell differentiation / positive regulation of protein polyubiquitination / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / negative regulation of granulocyte differentiation / Aberrant regulation of mitotic exit in cancer due to RB1 defects / negative regulation of monoatomic ion transmembrane transport ...regulation of lymphocyte differentiation / regulation of B cell proliferation / regulation of B cell differentiation / positive regulation of protein polyubiquitination / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / negative regulation of granulocyte differentiation / Aberrant regulation of mitotic exit in cancer due to RB1 defects / negative regulation of monoatomic ion transmembrane transport / Phosphorylation of the APC/C / Signaling by BMP / negative regulation of beige fat cell differentiation / cellular response to camptothecin / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / (E3-independent) E2 ubiquitin-conjugating enzyme / cullin-RING ubiquitin ligase complex / Cul7-RING ubiquitin ligase complex / cellular response to chemical stress / regulation of DNA damage checkpoint / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / positive regulation of protein autoubiquitination / positive regulation by virus of viral protein levels in host cell / regulation of nucleotide-excision repair / RNA polymerase II transcription initiation surveillance / protein neddylation / spindle assembly involved in female meiosis / NEDD8 ligase activity / epigenetic programming in the zygotic pronuclei / protein K27-linked ubiquitination / negative regulation of response to oxidative stress / VCB complex / UV-damage excision repair / Cul5-RING ubiquitin ligase complex / E2 ubiquitin-conjugating enzyme / ubiquitin-ubiquitin ligase activity / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / SCF ubiquitin ligase complex / biological process involved in interaction with symbiont / Cul2-RING ubiquitin ligase complex / limb development / regulation of mitotic cell cycle phase transition / Cul3-RING ubiquitin ligase complex / negative regulation of type I interferon production / WD40-repeat domain binding / Formation of the ternary complex, and subsequently, the 43S complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / Cul4A-RING E3 ubiquitin ligase complex / Prolactin receptor signaling / negative regulation of mitophagy / Cul4-RING E3 ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / Regulation of APC/C activators between G1/S and early anaphase / mesoderm development / Ribosomal scanning and start codon recognition / ubiquitin ligase complex scaffold activity / negative regulation of reproductive process / negative regulation of developmental process / Translation initiation complex formation / TGF-beta receptor signaling activates SMADs / ubiquitin conjugating enzyme activity / Transcriptional Regulation by VENTX / locomotory exploration behavior / hemopoiesis / regulation of proteolysis / T cell differentiation / somatic stem cell population maintenance / viral release from host cell / SARS-CoV-1 modulates host translation machinery / regulation of postsynapse assembly / Peptide chain elongation / negative regulation of BMP signaling pathway / cullin family protein binding / Selenocysteine synthesis / anatomical structure morphogenesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / ectopic germ cell programmed cell death / Viral mRNA Translation / protein monoubiquitination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / positive regulation of G1/S transition of mitotic cell cycle / GTP hydrolysis and joining of the 60S ribosomal subunit / positive regulation of Wnt signaling pathway / positive regulation of viral genome replication / L13a-mediated translational silencing of Ceruloplasmin expression / negative regulation of protein-containing complex assembly / Major pathway of rRNA processing in the nucleolus and cytosol / site of DNA damage / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / signal transduction in response to DNA damage / Nuclear events stimulated by ALK signaling in cancer / negative regulation of TORC1 signaling / protein K48-linked ubiquitination / transcription-coupled nucleotide-excision repair / negative regulation of insulin receptor signaling pathway / regulation of cellular response to insulin stimulus
Similarity search - Function
: / Nedd8-like ubiquitin / Yippee/Mis18/Cereblon / Yippee zinc-binding/DNA-binding /Mis18, centromere assembly / CULT domain / CULT domain profile. / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Lon N-terminal domain profile. / Lon protease, N-terminal domain ...: / Nedd8-like ubiquitin / Yippee/Mis18/Cereblon / Yippee zinc-binding/DNA-binding /Mis18, centromere assembly / CULT domain / CULT domain profile. / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Lon N-terminal domain profile. / Lon protease, N-terminal domain / Lon protease, N-terminal domain superfamily / ATP-dependent protease La (LON) substrate-binding domain / Found in ATP-dependent protease La (LON) / : / Cullin, N-terminal / Cullin protein neddylation domain / Cullin, conserved site / Cullin alpha solenoid domain / Cullin family signature. / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Cullin / : / Cullin alpha+beta domain / Cullin homology domain / Cullin homology domain superfamily / Cullin family profile. / : / RSE1/DDB1/CPSF1 second beta-propeller / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / : / CPSF A subunit region / RSE1/DDB1/CPSF1 first beta-propeller / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / PUA-like superfamily / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Zinc finger, C2H2 type / Ubiquitin-conjugating enzyme/RWD-like / zinc finger / Zinc finger C2H2 type domain profile. / S27a-like superfamily / Ribosomal protein S27a / Ribosomal protein S27a / Ribosomal protein S27a / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / Zinc finger RING-type profile. / Zinc finger, RING-type / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc-binding ribosomal protein / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 D1 / E3 ubiquitin-protein ligase RBX1 / Ubiquitin-ribosomal protein eS31 fusion protein / Cullin-4A / Ubiquitin-like protein NEDD8 / DNA damage-binding protein 1 / Protein cereblon / Zinc finger protein Aiolos
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.71 Å
AuthorsDeng ZH / Ai HS / Liu L
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)22137005, 92253302, 22227810, T2488301 China
CitationJournal: To Be Published
Title: Cryo-EM structure of cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
Authors: Deng ZH / Ai HS / Liu L
History
DepositionMay 17, 2025-
Header (metadata) releaseJun 10, 2026-
Map releaseJun 10, 2026-
UpdateJun 10, 2026-
Current statusJun 10, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_64663.png

Downloads & links

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Map

FileDownload / File: emd_64663.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 256 pix.
= 271.104 Å		1.06 Å/pix.
x 256 pix.
= 271.104 Å		1.06 Å/pix.
x 256 pix.
= 271.104 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.059 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0919
Minimum - Maximum-0.6001643 - 1.0280254
Average (Standard dev.)-0.00015265525 (±0.035887543)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 271.104 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_64663_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_64663_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubi...

EntireName: Cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
Components
  • Complex: Cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
    • Protein or peptide: Cullin-4A
    • Protein or peptide: DNA damage-binding protein 1
    • Protein or peptide: Protein cereblon
    • Protein or peptide: Ubiquitin-conjugating enzyme E2 D1
    • Protein or peptide: Zinc finger protein Aiolos
    • Protein or peptide: NEDD8
    • Protein or peptide: E3 ubiquitin-protein ligase RBX1, N-terminally processed
    • Protein or peptide: Ubiquitin
  • Ligand: Cemsidomide
  • Ligand: ZINC ION

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Supramolecule #1: Cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubi...

SupramoleculeName: Cemsidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Cullin-4A

MacromoleculeName: Cullin-4A / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 89.368867 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GPGSGWSHPQ FEKGSGSADE APRKGSFSAL VGRTNGLTKP AALAAAPAKP GGAGGSKKLV IKNFRDRPRL PDNYTQDTWR KLHEAVRAV QSSTSIRYNL EELYQAVENL CSHKVSPMLY KQLRQACEDH VQAQILPFRE DSLDSVLFLK KINTCWQDHC R QMIMIRSI ...String:
GPGSGWSHPQ FEKGSGSADE APRKGSFSAL VGRTNGLTKP AALAAAPAKP GGAGGSKKLV IKNFRDRPRL PDNYTQDTWR KLHEAVRAV QSSTSIRYNL EELYQAVENL CSHKVSPMLY KQLRQACEDH VQAQILPFRE DSLDSVLFLK KINTCWQDHC R QMIMIRSI FLFLDRTYVL QNSTLPSIWD MGLELFRTHI ISDKMVQSKT IDGILLLIER ERSGEAVDRS LLRSLLGMLS DL QVYKDSF ELKFLEETNC LYAAEGQRLM QEREVPEYLN HVSKRLEEEG DRVITYLDHS TQKPLIACVE KQLLGEHLTA ILQ KGLDHL LDENRVPDLA QMYQLFSRVR GGQQALLQHW SEYIKTFGTA IVINPEKDKD MVQDLLDFKD KVDHVIEVCF QKNE RFVNL MKESFETFIN KRPNKPAELI AKHVDSKLRA GNKEATDEEL ERTLDKIMIL FRFIHGKDVF EAFYKKDLAK RLLVG KSAS VDAEKSMLSK LKHECGAAFT SKLEGMFKDM ELSKDIMVHF KQHMQNQSDS GPIDLTVNIL TMGYWPTYTP MEVHLT PEM IKLQEVFKAF YLGKHSGRKL QWQTTLGHAV LKAEFKEGKK EFQVSLFQTL VLLMFNEGDG FSFEEIKMAT GIEDSEL RR TLQSLACGKA RVLIKSPKGK EVEDGDKFIF NGEFKHKLFR IKINQIQMKE TVEEQVSTTE RVFQDRQYQI DAAIVRIM K MRKTLGHNLL VSELYNQLKF PVKPGDLKKR IESLIDRDYM ERDKDNPNQY HYVA

UniProtKB: Cullin-4A

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Macromolecule #2: DNA damage-binding protein 1

MacromoleculeName: DNA damage-binding protein 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 127.097469 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACIL EYKQSGESID IITRAHGNVQ DRIGRPSETG IIGIIDPECR MIGLRLYDGL FKVIPLDRDN KELKAFNIRL E ELHVIDVK ...String:
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACIL EYKQSGESID IITRAHGNVQ DRIGRPSETG IIGIIDPECR MIGLRLYDGL FKVIPLDRDN KELKAFNIRL E ELHVIDVK FLYGCQAPTI CFVYQDPQGR HVKTYEVSLR EKEFNKGPWK QENVEAEASM VIAVPEPFGG AIIIGQESIT YH NGDKYLA IAPPIIKQST IVCHNRVDPN GSRYLLGDME GRLFMLLLEK EEQMDGTVTL KDLRVELLGE TSIAECLTYL DNG VVFVGS RLGDSQLVKL NVDSNEQGSY VVAMETFTNL GPIVDMCVVD LERQGQGQLV TCSGAFKEGS LRIIRNGIGI HEHA SIDLP GIKGLWPLRS DPNRETDDTL VLSFVGQTRV LMLNGEEVEE TELMGFVDDQ QTFFCGNVAH QQLIQITSAS VRLVS QEPK ALVSEWKEPQ AKNISVASCN SSQVVVAVGR ALYYLQIHPQ ELRQISHTEM EHEVACLDIT PLGDSNGLSP LCAIGL WTD ISARILKLPS FELLHKEMLG GEIIPRSILM TTFESSHYLL CALGDGALFY FGLNIETGLL SDRKKVTLGT QPTVLRT FR SLSTTNVFAC SDRPTVIYSS NHKLVFSNVN LKEVNYMCPL NSDGYPDSLA LANNSTLTIG TIDEIQKLHI RTVPLYES P RKICYQEVSQ CFGVLSSRIE VQDTSGGTTA LRPSASTQAL SSSVSSSKLF SSSTAPHETS FGEEVEVHNL LIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVR LYEWTTEKEL RTECNHYNNI MALYLKTKGD FILVGDLMRS VLLLAYKPME GNFEEIARDF NPNWMSAVEI L DDDNFLGA ENAFNLFVCQ KDSAATTDEE RQHLQEVGLF HLGEFVNVFC HGSLVMQNLG ETSTPTQGSV LFGTVNGMIG LV TSLSESW YNLLLDMQNR LNKVIKSVGK IEHSFWRSFH TERKTEPATG FIDGDLIESF LDISRPKMQE VVANLQYDDG SGM KREATA DDLIKVVEEL TRIH

UniProtKB: DNA damage-binding protein 1

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Macromolecule #3: Protein cereblon

MacromoleculeName: Protein cereblon / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 48.874941 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GSSHHHHHHH HSSGLEVLFQ GPGSSAKKPN IINFDTSLPT SHTYLGADME EFHGRTLHDD DSCQVIPVLP QVMMILIPGQ TLPLQLFHP QEVSMVRNLI QKDRTFAVLA YSNVQEREAQ FGTTAEIYAY REEQDFGIEI VKVKAIGRQR FKVLELRTQS D GIQQAKVQ ...String:
GSSHHHHHHH HSSGLEVLFQ GPGSSAKKPN IINFDTSLPT SHTYLGADME EFHGRTLHDD DSCQVIPVLP QVMMILIPGQ TLPLQLFHP QEVSMVRNLI QKDRTFAVLA YSNVQEREAQ FGTTAEIYAY REEQDFGIEI VKVKAIGRQR FKVLELRTQS D GIQQAKVQ ILPECVLPST MSAVQLESLN KCQIFPSKPV SREDQCSYKW WQKYQKRKFH CANLTSWPRW LYSLYDAETL MD RIKKQLR EWDENLKDDS LPSNPIDFSY RVAACLPIDD VLRIQLLKIG SAIQRLRCEL DIMNKCTSLC CKQCQETEIT TKN EIFSLS LCGPMAAYVN PHGYVHETLT VYKACNLNLI GRPSTEHSWF PGYAWTVAQC KICASHIGWK FTATKKDMSP QKFW GLTRS ALLPTIPDTE DEISPDKVIL CL

UniProtKB: Protein cereblon

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Macromolecule #4: Ubiquitin-conjugating enzyme E2 D1

MacromoleculeName: Ubiquitin-conjugating enzyme E2 D1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: E2 ubiquitin-conjugating enzyme
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.490812 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
ALKRIQKELS DLQRDPPAHC SAGPVGDDLF HWQATIMGPP DSAYQGGVFF LTVHFPTDYP FKPPKIAFTT KIYHPNINSN GSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV PDIAQIYKSD KEKYNRHARE WTQKYAM

UniProtKB: Ubiquitin-conjugating enzyme E2 D1

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Macromolecule #5: Zinc finger protein Aiolos

MacromoleculeName: Zinc finger protein Aiolos / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 6.549474 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GPGERPFQCN QCGASFTQKG NLLRHICLHT GEKPFKCHLC NYATQRRDAL TGHLRTHS

UniProtKB: Zinc finger protein Aiolos

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Macromolecule #6: NEDD8

MacromoleculeName: NEDD8 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.573978 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MLIKVKTLTG KEIEIDIEPT DKVERIKERV EEKEGIPPQQ QRLIYSGKQM NDEKTAADYK ILGGSVLHLV LALRGG

UniProtKB: Ubiquitin-like protein NEDD8

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Macromolecule #7: E3 ubiquitin-protein ligase RBX1, N-terminally processed

MacromoleculeName: E3 ubiquitin-protein ligase RBX1, N-terminally processed
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.457076 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GPGSAAAMDV DTPSGTNSGA GKKRFEVKKW NAVALWAWDI VVDNCAICRN HIMDLCIECQ ANQASATSEE CTVAWGVCNH AFHFHCISR WLKTRQVCPL DNREWEFQKY GH

UniProtKB: E3 ubiquitin-protein ligase RBX1

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Macromolecule #8: Ubiquitin

MacromoleculeName: Ubiquitin / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.576831 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

UniProtKB: Ubiquitin-ribosomal protein eS31 fusion protein

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Macromolecule #9: Cemsidomide

MacromoleculeName: Cemsidomide / type: ligand / ID: 9 / Number of copies: 1 / Formula: A1EQO
Molecular weightTheoretical: 469.532 Da

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Macromolecule #10: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 10 / Number of copies: 6 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k 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: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.71 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1.1) / Number images used: 48755
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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