+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17539 | ||||||||||||
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Title | Cryo-EM structure of dimeric UBR5 | ||||||||||||
Map data | Amplitude-scaled map (LocScale). | ||||||||||||
Sample |
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Keywords | E3 / ubiquitin ligase / HECT / LIGASE | ||||||||||||
Function / homology | Function and homology information heterochromatin boundary formation / HECT-type E3 ubiquitin transferase / DNA repair-dependent chromatin remodeling / ubiquitin-ubiquitin ligase activity / progesterone receptor signaling pathway / protein K48-linked ubiquitination / ubiquitin binding / protein polyubiquitination / positive regulation of protein import into nucleus / positive regulation of canonical Wnt signaling pathway ...heterochromatin boundary formation / HECT-type E3 ubiquitin transferase / DNA repair-dependent chromatin remodeling / ubiquitin-ubiquitin ligase activity / progesterone receptor signaling pathway / protein K48-linked ubiquitination / ubiquitin binding / protein polyubiquitination / positive regulation of protein import into nucleus / positive regulation of canonical Wnt signaling pathway / ubiquitin protein ligase activity / DNA repair / DNA damage response / positive regulation of gene expression / perinuclear region of cytoplasm / protein-containing complex / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.36 Å | ||||||||||||
Authors | Aguirre JD / Kater L / Kempf G / Cavadini S / Thoma NH | ||||||||||||
Funding support | Switzerland, European Union, 3 items
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Citation | Journal: To Be Published Title: UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability Authors: Na NA | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17539.map.gz | 106.6 MB | EMDB map data format | |
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Header (meta data) | emd-17539-v30.xml emd-17539.xml | 18.2 KB 18.2 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17539_fsc.xml | 12.7 KB | Display | FSC data file |
Images | emd_17539.png | 60.3 KB | ||
Others | emd_17539_additional_1.map.gz emd_17539_half_map_1.map.gz emd_17539_half_map_2.map.gz | 106.8 MB 200.2 MB 200.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17539 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17539 | HTTPS FTP |
-Related structure data
Related structure data | 8p82MC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_17539.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Amplitude-scaled map (LocScale). | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.118 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Full map.
File | emd_17539_additional_1.map | ||||||||||||
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Annotation | Full map. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-map A.
File | emd_17539_half_map_1.map | ||||||||||||
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Annotation | Half-map A. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-map B.
File | emd_17539_half_map_2.map | ||||||||||||
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Annotation | Half-map B. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Dimer of UBR5
Entire | Name: Dimer of UBR5 |
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Components |
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-Supramolecule #1: Dimer of UBR5
Supramolecule | Name: Dimer of UBR5 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: E3 ubiquitin-protein ligase UBR5
Macromolecule | Name: E3 ubiquitin-protein ligase UBR5 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: HECT-type E3 ubiquitin transferase |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 313.263688 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MDYKDDDDKL AAANSSIDLI STSLYKKAGF RTMTSIHFVV HPLPGTEDQL NDRLREVSEK LNKYNLNSHP PLNVLEQATI KQCVVGPNH AAFLLEDGRV CRIGFSVQPD RLELGKPDNN DGSKLNSNSG AGRTSRPGRT SDSPWFLSGS ETLGRLAGNT L GSRWSSGV ...String: MDYKDDDDKL AAANSSIDLI STSLYKKAGF RTMTSIHFVV HPLPGTEDQL NDRLREVSEK LNKYNLNSHP PLNVLEQATI KQCVVGPNH AAFLLEDGRV CRIGFSVQPD RLELGKPDNN DGSKLNSNSG AGRTSRPGRT SDSPWFLSGS ETLGRLAGNT L GSRWSSGV GGSGGGSSGR SSAGARDSRR QTRVIRTGRD RGSGLLGSQP QPVIPASVIP EELISQAQVV LQGKSRSVII RE LQRTNLD VNLAVNNLLS RDDEDGDDGD DTASESYLPG EDLMSLLDAD IHSAHPSVII DADAMFSEDI SYFGYPSFRR SSL SRLGSS RVLLLPLERD SELLRERESV LRLRERRWLD GASFDNERGS TSKEGEPNLD KKNTPVQSPV SLGEDLQWWP DKDG TKFIC IGALYSELLA VSSKGELYQW KWSESEPYRN AQNPSLHHPR ATFLGLTNEK IVLLSANSIR ATVATENNKV ATWVD ETLS SVASKLEHTA QTYSELQGER IVSLHCCALY TCAQLENSLY WWGVVPFSQR KKMLEKARAK NKKPKSSAGI SSMPNI TVG TQVCLRNNPL YHAGAVAFSI SAGIPKVGVL MESVWNMNDS CRFQLRSPES LKNMEKASKT TEAKPESKQE PVKTEMG PP PSPASTCSDA SSIASSASMP YKRRRSTPAP KEEEKVNEEQ WSLREVVFVE DVKNVPVGKV LKVDGAYVAV KFPGTSSN T NCQNSSGPDA DPSSLLQDCR LLRIDELQVV KTGGTPKVPD CFQRTPKKLC IPEKTEILAV NVDSKGVHAV LKTGNWVRY CIFDLATGKA EQENNFPTSS IAFLGQNERN VAIFTAGQES PIILRDGNGT IYPMAKDCMG GIRDPDWLDL PPISSLGMGV HSLINLPAN STIKKKAAVI IMAVEKQTLM QHILRCDYEA CRQYLMNLEQ AVVLEQNLQM LQTFISHRCD GNRNILHACV S VCFPTSNK ETKEEEEAER SERNTFAERL SAVEAIANAI SVVSSNGPGN RAGSSSSRSL RLREMMRRSL RAAGLGRHEA GA SSSDHQD PVSPPIAPPS WVPDPPAMDP DGDIDFILAP AVGSLTTAAT GTGQGPSTST IPGPSTEPSV VESKDRKANA HFI LKLLCD SVVLQPYLRE LLSAKDARGM TPFMSAVSGR AYPAAITILE TAQKIAKAEI SSSEKEEDVF MGMVCPSGTN PDDS PLYVL CCNDTCSFTW TGAEHINQDI FECRTCGLLE SLCCCTECAR VCHKGHDCKL KRTSPTAYCD CWEKCKCKTL IAGQK SARL DLLYRLLTAT NLVTLPNSRG EHLLLFLVQT VARQTVEHCQ YRPPRIREDR NRKTASPEDS DMPDHDLEPP RFAQLA LER VLQDWNALKS MIMFGSQENK DPLSASSRIG HLLPEEQVYL NQQSGTIRLD CFTHCLIVKC TADILLLDTL LGTLVKE LQ NKYTPGRREE AIAVTMRFLR SVARVFVILS VEMASSKKKN NFIPQPIGKC KRVFQALLPY AVEELCNVAE SLIVPVRM G IARPTAPFTL ASTSIDAMQG SEELFSVEPL PPRPSSDQSS SSSQSQSSYI IRNPQQRRIS QSQPVRGRDE EQDDIVSAD VEEVEVVEGV AGEEDHHDEQ EEHGEENAEA EGQHDEHDED GSDMELDLLA AAETESDSES NHSNQDNASG RRSVVTAATA GSEAGASSV PAFFSEDDSQ SNDSSDSDSS SSQSDDIEQE TFMLDEPLER TTNSSHANGA AQAPRSMQWA VRNTQHQRAA S TAPSSTST PAASSAGLIY IDPSNLRRSG TISTSAAAAA AALEASNASS YLTSASSLAR AYSIVIRQIS DLMGLIPKYN HL VYSQIPA AVKLTYQDAV NLQNYVEEKL IPTWNWMVSI MDSTEAQLRY GSALASAGDP GHPNHPLHAS QNSARRERMT ARE EASLRT LEGRRRATLL SARQGMMSAR GDFLNYALSL MRSHNDEHSD VLPVLDVCSL KHVAYVFQAL IYWIKAMNQQ TTLD TPQLE RKRTRELLEL GIDNEDSEHE NDDDTNQSAT LNDKDDDSLP AETGQNHPFF RRSDSMTFLG CIPPNPFEVP LAEAI PLAD QPHLLQPNAR KEDLFGRPSQ GLYSSSASSG KCLMEVTVDR NCLEVLPTKM SYAANLKNVM NMQNRQKKEG EEQPVL PEE TESSKPGPSA HDLAAQLKSS LLAEIGLTES EGPPLTSFRP QCSFMGMVIS HDMLLGRWRL SLELFGRVFM EDVGAEP GS ILTELGGFEV KESKFRREME KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEG S GVARSFYTAI AQAFLSNEKL PNLECIQNAN KGTHTSLMQR LRNRGERDRE REREREMRRS SGLRAGSRRD RDRDFRRQL SIDTRPFRPA SEGNPSDDPE PLPAHRQALG ERLYPRVQAM QPAFASKITG MLLELSPAQL LLLLASEDSL RARVDEAMEL IIAHGRENG ADSILDLGLV DSSEKVQQEN RKRHGSSRSV VDMDLDDTDD GDDNAPLFYQ PGKRGFYTPR PGKNTEARLN C FRNIGRIL GLCLLQNELC PITLNRHVIK VLLGRKVNWH DFAFFDPVMY ESLRQLILAS QSSDADAVFS AMDLAFAIDL CK EEGGGQV ELIPNGVNIP VTPQNVYEYV RKYAEHRMLV VAEQPLHAMR KGLLDVLPKN SLEDLTAEDF RLLVNGCGEV NVQ MLISFT SFNDESGENA EKLLQFKRWF WSIVEKMSMT ERQDLVYFWT SSPSLPASEE GFQPMPSITI RPPDDQHLPT ANTC ISRLY VPLYSSKQIL KQKLLLAIKT KNFGFV |
-Macromolecule #2: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 2 / Number of copies: 6 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.6 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.0 µm |
Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
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Output model | PDB-8p82: |