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- EMDB-44630: human CRL2-ZYG11B complex -

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Basic information

Entry
Database: EMDB / ID: EMD-44630
Titlehuman CRL2-ZYG11B complex
Map data
Sample
  • Complex: human CRL2-ZYG11B
    • Complex: ZYG11B
      • Protein or peptide: Protein zyg-11 homolog B
    • Complex: Elongin-B/Elongin-C
      • Protein or peptide: Elongin-B
      • Protein or peptide: Elongin-C
    • Complex: Cullin-2/E3 ubiquitin-protein ligase RBX1
      • Protein or peptide: Cullin-2
      • Protein or peptide: E3 ubiquitin-protein ligase RBX1
  • Ligand: ZINC ION
KeywordsE3 ligase complex / peptide binding / PEPTIDE BINDING PROTEIN
Function / homology
Function and homology information


negative regulation of beige fat cell differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / cullin-RING ubiquitin ligase complex / Cul7-RING ubiquitin ligase complex / cellular response to chemical stress / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / protein K27-linked ubiquitination / target-directed miRNA degradation / elongin complex ...negative regulation of beige fat cell differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / cullin-RING ubiquitin ligase complex / Cul7-RING ubiquitin ligase complex / cellular response to chemical stress / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / protein K27-linked ubiquitination / target-directed miRNA degradation / elongin complex / positive regulation of protein autoubiquitination / RNA polymerase II transcription initiation surveillance / protein neddylation / NEDD8 ligase activity / negative regulation of response to oxidative stress / VCB complex / Cul5-RING ubiquitin ligase complex / ubiquitin-ubiquitin ligase activity / SCF ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / negative regulation of type I interferon production / Cul2-RING ubiquitin ligase complex / Cul3-RING ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / negative regulation of mitophagy / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / Prolactin receptor signaling / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / 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 / cullin family protein binding / protein monoubiquitination / 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 / site of DNA damage / protein K48-linked ubiquitination / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / signal transduction in response to DNA damage / Nuclear events stimulated by ALK signaling in cancer / transcription-coupled nucleotide-excision repair / regulation of cellular response to insulin stimulus / RNA Polymerase II Pre-transcription Events / positive regulation of TORC1 signaling / negative regulation of insulin receptor signaling pathway / post-translational protein modification / intrinsic apoptotic signaling pathway / Regulation of BACH1 activity / T cell activation / transcription corepressor binding / negative regulation of canonical NF-kappaB signal transduction / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / cellular response to amino acid stimulus / Degradation of DVL / Degradation of CRY and PER proteins / G1/S transition of mitotic cell cycle / Degradation of GLI1 by the proteasome / negative regulation of canonical Wnt signaling pathway / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / Hedgehog 'on' state / Recognition of DNA damage by PCNA-containing replication complex / Vif-mediated degradation of APOBEC3G / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / RING-type E3 ubiquitin transferase / Inactivation of CSF3 (G-CSF) signaling / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / DNA Damage Recognition in GG-NER / NOTCH1 Intracellular Domain Regulates Transcription / Evasion by RSV of host interferon responses / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Regulation of expression of SLITs and ROBOs / Interleukin-1 signaling / Formation of Incision Complex in GG-NER / Orc1 removal from chromatin / Regulation of RAS by GAPs / Dual incision in TC-NER / protein polyubiquitination / Regulation of RUNX2 expression and activity / Gap-filling DNA repair synthesis and ligation in TC-NER / positive regulation of protein catabolic process / ubiquitin-protein transferase activity / cellular response to UV / ubiquitin protein ligase activity
Similarity search - Function
: / : / Protein zer-1 homolog-like, C-terminal domain / Zer-1-like, Leucine-rich repeats / : / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / : / Cullin alpha+beta domain / Cullin protein neddylation domain ...: / : / Protein zer-1 homolog-like, C-terminal domain / Zer-1-like, Leucine-rich repeats / : / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / : / Cullin alpha+beta domain / Cullin protein neddylation domain / : / Cullin, conserved site / Cullin family signature. / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Cullin, N-terminal / Elongin-C / Elongin B / Cullin alpha solenoid domain / Cullin / Cullin homology domain / Cullin homology domain superfamily / Cullin family profile. / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / Leucine-rich repeat profile. / SKP1/BTB/POZ domain superfamily / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / Armadillo-like helical / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Armadillo-type fold / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
E3 ubiquitin-protein ligase RBX1 / Cullin-2 / Elongin-C / Elongin-B / Protein zyg-11 homolog B
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.78 Å
AuthorsLiu X / Gross JD
Funding support United States, 1 items
OrganizationGrant numberCountry
Other private United States
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.
Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams /
Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
History
DepositionApr 25, 2024-
Header (metadata) releaseMar 18, 2026-
Map releaseMar 18, 2026-
UpdateMar 18, 2026-
Current statusMar 18, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_44630.png

Downloads & links

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Map

FileDownload / File: emd_44630.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
0.84 Å/pix.
x 360 pix.
= 300.6 Å		0.84 Å/pix.
x 360 pix.
= 300.6 Å		0.84 Å/pix.
x 360 pix.
= 300.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.835 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy EMDB: 0.7
Minimum - Maximum-34.758743000000003 - 56.450104000000003
Average (Standard dev.)0.000000000000421 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 300.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_44630_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_44630_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : human CRL2-ZYG11B

EntireName: human CRL2-ZYG11B
Components
  • Complex: human CRL2-ZYG11B
    • Complex: ZYG11B
      • Protein or peptide: Protein zyg-11 homolog B
    • Complex: Elongin-B/Elongin-C
      • Protein or peptide: Elongin-B
      • Protein or peptide: Elongin-C
    • Complex: Cullin-2/E3 ubiquitin-protein ligase RBX1
      • Protein or peptide: Cullin-2
      • Protein or peptide: E3 ubiquitin-protein ligase RBX1
  • Ligand: ZINC ION

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Supramolecule #1: human CRL2-ZYG11B

SupramoleculeName: human CRL2-ZYG11B / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Molecular weightTheoretical: 230 kDa/nm

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Supramolecule #2: ZYG11B

SupramoleculeName: ZYG11B / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Elongin-B/Elongin-C

SupramoleculeName: Elongin-B/Elongin-C / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Cullin-2/E3 ubiquitin-protein ligase RBX1

SupramoleculeName: Cullin-2/E3 ubiquitin-protein ligase RBX1 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #4-#5
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Protein zyg-11 homolog B

MacromoleculeName: Protein zyg-11 homolog B / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 84.463344 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: SHMVDPEDQA GAAMEEASPY SLLDICLNFL TTHLEKFCSA RQDGTLCLQE PGVFPQEVAD RLLRTMAFHG LLNDGTVGIF RGNQMRLKR ACIRKAKISA VAFRKAFCHH KLVELDATGV NADITITDII SGLGSNKWIQ QNLQCLVLNS LTLSLEDPYE R CFSRLSGL ...String:
SHMVDPEDQA GAAMEEASPY SLLDICLNFL TTHLEKFCSA RQDGTLCLQE PGVFPQEVAD RLLRTMAFHG LLNDGTVGIF RGNQMRLKR ACIRKAKISA VAFRKAFCHH KLVELDATGV NADITITDII SGLGSNKWIQ QNLQCLVLNS LTLSLEDPYE R CFSRLSGL RALSITNVLF YNEDLAEVAS LPRLESLDIS NTSITDITAL LACKDRLKSL TMHHLKCLKM TTTQILDVVR EL KHLNHLD ISDDKQFTSD IALRLLEQKD ILPNLVSLDV SGRKHVTDKA VEAFIQQRPS MQFVGLLATD AGYSEFLTGE GHL KVSGEA NETQIAEALK RYSERAFFVR EALFHLFSLT HVMEKTKPEI LKLVVTGMRN HPMNLPVQLA ASACVFNLTK QDLA AGMPV RLLADVTHLL LKAMEHFPNH QQLQKNCLLS LCSDRILQDV PFNRFEAAKL VMQWLCNHED QNMQRMAVAI ISILA AKLS TEQTAQLGTE LFIVRQLLQI VKQKTNQNSV DTTLKFTLSA LWNLTDESPT TCRHFIENQG LELFMRVLES FPTESS IQQ KVLGLLNNIA EVQELHSELM WKDFIDHISS LLHSVEVEVS YFAAGIIAHL ISRGEQAWTL SRSQRNSLLD DLHSAIL KW PTPECEMVAY RSFNPFFPLL GCFTTPGVQL WAVWAMQHVC SKNPSRYCSM LIEEGGLQHL YNIKDHEHTD PHVQQIAV A ILDSLEKHIV RHGRPPPCKK QPQARLN

UniProtKB: Protein zyg-11 homolog B

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Macromolecule #2: Elongin-B

MacromoleculeName: Elongin-B / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.147781 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALC IEPFSSPPEL PDVMKPQDSG SSANEQAVQ

UniProtKB: Elongin-B

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Macromolecule #3: Elongin-C

MacromoleculeName: Elongin-C / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.84342 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MYVKLISSDG HEFIVKREHA LTSGTIKAML SGPGQFAENE TNEVNFREIP SHVLSKVCMY FTYKVRYTNS STEIPEFPIA PEIALELLM AANFLDC

UniProtKB: Elongin-C

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Macromolecule #4: Cullin-2

MacromoleculeName: Cullin-2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 86.967734 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: SLKPRVVDFD ETWNKLLTTI KAVVMLEYVE RATWNDRFSD IYALCVAYPE PLGERLYTET KIFLENHVRH LHKRVLESEE QVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI R MLLREIKN ...String:
SLKPRVVDFD ETWNKLLTTI KAVVMLEYVE RATWNDRFSD IYALCVAYPE PLGERLYTET KIFLENHVRH LHKRVLESEE QVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI R MLLREIKN DRGGEDPNQK VIHGVINSFV HVEQYKKKFP LKFYQEIFES PFLTETGEYY KQEASNLLQE SNCSQYMEKV LG RLKDEEI RCRKYLHPSS YTKVIHECQQ RMVADHLQFL HAECHNIIRQ EKKNDMANMY VLLRAVSTGL PHMIQELQNH IHD EGLRAT SNLTQENMPT LFVESVLEVH GKFVQLINTV LNGDQHFMSA LDKALTSVVN YREPKSVCKA PELLAKYCDN LLKK SAKGM TENEVEDRLT SFITVFKYID DKDVFQKFYA RMLAKRLIHG LSMSMDSEEA MINKLKQACG YEFTSKLHRM YTDMS VSAD LNNKFNNFIK NQDTVIDLGI SFQIYVLQAG AWPLTQAPSS TFAIPQELEK SVQMFELFYS QHFSGRKLTW LHYLCT GEV KMNYLGKPYV AMVTTYQMAV LLAFNNSETV SYKELQDSTQ MNEKELTKTI KSLLDVKMIN HDSEKEDIDA ESSFSLN MN FSSKRTKFKI TTSMQKDTPQ EMEQTRSAVD EDRKMYLQAA IVRIMKARKV LRHNALIQEV ISQSRARFNP SISMIKKC I EVLIDKQYIE RSQASADEYS YVA

UniProtKB: Cullin-2

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Macromolecule #5: E3 ubiquitin-protein ligase RBX1

MacromoleculeName: E3 ubiquitin-protein ligase RBX1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.289977 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLK TRQVCPLDNR EWEFQKYGH

UniProtKB: E3 ubiquitin-protein ligase RBX1

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Macromolecule #6: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 6 / Number of copies: 3 / 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: 7.2
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300
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: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: 4D-STEM / Nominal defocus max: 5.0 µm / Nominal defocus min: 1.0 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
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 reconstructionAlgorithm: ALGEBRAIC (ARTS) / Resolution.type: BY AUTHOR / Resolution: 3.78 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4) / Number images used: 177561
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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