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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | monomeric ZYG11B-EloB-EloC + substrate peptide GYIND | |||||||||
Map data | ||||||||||
Sample |
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Keywords | monomeric ZYG11B-EloB-EloC with substrate peptide GYIND / LIGASE | |||||||||
| Function / homology | Function and homology informationtarget-directed miRNA degradation / elongin complex / VCB complex / Cul5-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Cul2-RING ubiquitin ligase complex / protein quality control for misfolded or incompletely synthesized proteins / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery ...target-directed miRNA degradation / elongin complex / VCB complex / Cul5-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Cul2-RING ubiquitin ligase complex / protein quality control for misfolded or incompletely synthesized proteins / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / bioluminescence / transcription corepressor binding / generation of precursor metabolites and energy / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Evasion by RSV of host interferon responses / Regulation of expression of SLITs and ROBOs / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Neddylation / protein-containing complex assembly / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity / protein ubiquitination / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / nucleoplasm / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.37 Å | |||||||||
Authors | Lin N / Wang Y / Gao P | |||||||||
| Funding support | China, 1 items
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Citation | Journal: To Be PublishedTitle: Structure of monomeric ZYG11B-EloB-EloC with substrate peptide GYIND at 3.37 Angstroms resolution. Authors: Lin N / Wang Y / Gao P | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_63161.map.gz | 230.1 MB | EMDB map data format | |
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| Header (meta data) | emd-63161-v30.xml emd-63161.xml | 18.4 KB 18.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_63161_fsc.xml | 13.2 KB | Display | FSC data file |
| Images | emd_63161.png | 58.5 KB | ||
| Filedesc metadata | emd-63161.cif.gz | 6.2 KB | ||
| Others | emd_63161_half_map_1.map.gz emd_63161_half_map_2.map.gz | 226.8 MB 226.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63161 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63161 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9lk2MC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_63161.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.8 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_63161_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_63161_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : monomeric ZYG11B-EloB-EloC + susbstrate peptide GYIND
| Entire | Name: monomeric ZYG11B-EloB-EloC + susbstrate peptide GYIND |
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| Components |
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-Supramolecule #1: monomeric ZYG11B-EloB-EloC + susbstrate peptide GYIND
| Supramolecule | Name: monomeric ZYG11B-EloB-EloC + susbstrate peptide GYIND / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Protein zyg-11 homolog B,Green fluorescent protein
| Macromolecule | Name: Protein zyg-11 homolog B,Green fluorescent protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 113.848242 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MPEDQAGAAM EEASPYSLLD ICLNFLTTHL EKFCSARQDG TLCLQEPGVF PQEVADRLLR TMAFHGLLND GTVGIFRGNQ MRLKRACIR KAKISAVAFR KAFCHHKLVE LDATGVNADI TITDIISGLG SNKWIQQNLQ CLVLNSLTLS LEDPYERCFS R LSGLRALS ...String: MPEDQAGAAM EEASPYSLLD ICLNFLTTHL EKFCSARQDG TLCLQEPGVF PQEVADRLLR TMAFHGLLND GTVGIFRGNQ MRLKRACIR KAKISAVAFR KAFCHHKLVE LDATGVNADI TITDIISGLG SNKWIQQNLQ CLVLNSLTLS LEDPYERCFS R LSGLRALS ITNVLFYNED LAEVASLPRL ESLDISNTSI TDITALLACK DRLKSLTMHH LKCLKMTTTQ ILDVVRELKH LN HLDISDD KQFTSDIALR LLEQKDILPN LVSLDVSGRK HVTDKAVEAF IQQRPSMQFV GLLATDAGYS EFLTGEGHLK VSG EANETQ IAEALKRYSE RAFFVREALF HLFSLTHVME KTKPEILKLV VTGMRNHPMN LPVQLAASAC VFNLTKQDLA AGMP VRLLA DVTHLLLKAM EHFPNHQQLQ KNCLLSLCSD RILQDVPFNR FEAAKLVMQW LCNHEDQNMQ RMAVAIISIL AAKLS TEQT AQLGTELFIV RQLLQIVKQK TNQNSVDTTL KFTLSALWNL TDESPTTCRH FIENQGLELF MRVLESFPTE SSIQQK VLG LLNNIAEVQE LHSELMWKDF IDHISSLLHS VEVEVSYFAA GIIAHLISRG EQAWTLSRSQ RNSLLDDLHS AILKWPT PE CEMVAYRSFN PFFPLLGCFT TPGVQLWAVW AMQHVCSKNP SRYCSMLIEE GGLQHLYNIK DHEHTDPHVQ QIAVAILD S LEKHIVRHGR PPPCKKQPQA RLNKLGSENL YFQGGSGSKG EELFTGVVPI LVELDGDVNG HKFSVSGEGE GDATYGKLT LKFICTTGKL PVPWPTLVTT LTYGVQCFSR YPDHMKRHDF FKSAMPEGYV QERTISFKDD GNYKTRAEVK FEGDTLVNRI ELKGIDFKE DGNILGHKLE YNYNSHNVYI TADKQKNGIK ANFKIRHNIE DGSVQLADHY QQNTPIGDGP VLLPDNHYLS T QSALSKDP NEKRDHMVLL EFVTAAGITH GMDELYKGSG HHHHHHHHHH H UniProtKB: Protein zyg-11 homolog B, Green fluorescent protein |
-Macromolecule #2: Elongin-B
| Macromolecule | Name: Elongin-B / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 15.393124 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: HHHHHHHHGS ENLYFQGGSM DVFLMIRRHK TTIFTDAKES STVFELKRIV EGILKRPPDE QRLYKDDQLL DDGKTLGECG FTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ UniProtKB: Elongin-B |
-Macromolecule #3: Elongin-C
| Macromolecule | Name: Elongin-C / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 12.485135 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTE IPEFPIAPEI ALELLMAANF LDC UniProtKB: Elongin-C |
-Macromolecule #4: GLY-TYR-ILE-ASN-ASP
| Macromolecule | Name: GLY-TYR-ILE-ASN-ASP / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 580.589 Da |
| Sequence | String: GYIND |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TECNAI ARCTICA |
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| Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation

















Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN

