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Yorodumi- PDB-9w39: Structure of human 26S proteasome complexed with midnolin, 19S pr... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9w39 | ||||||||||||||||||||||||
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| Title | Structure of human 26S proteasome complexed with midnolin, 19S proteasome with Ubl bound | ||||||||||||||||||||||||
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Keywords | HYDROLASE / proteasome / midnolin | ||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of glucokinase activity / thyrotropin-releasing hormone receptor binding / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / nuclear proteasome complex / host-mediated perturbation of viral transcription / positive regulation of inclusion body assembly / integrator complex / proteasome accessory complex / meiosis I ...negative regulation of glucokinase activity / thyrotropin-releasing hormone receptor binding / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / nuclear proteasome complex / host-mediated perturbation of viral transcription / positive regulation of inclusion body assembly / integrator complex / proteasome accessory complex / meiosis I / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / protein K63-linked deubiquitination / negative regulation of programmed cell death / Regulation of ornithine decarboxylase (ODC) / metal-dependent deubiquitinase activity / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / K63-linked deubiquitinase activity / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / transcription factor binding / Resolution of D-loop Structures through Holliday Junction Intermediates / detection of maltose stimulus / proteasome binding / maltose transport complex / Impaired BRCA2 binding to RAD51 / regulation of protein catabolic process / carbohydrate transport / proteasome storage granule / proteasomal ubiquitin-independent protein catabolic process / Presynaptic phase of homologous DNA pairing and strand exchange / general transcription initiation factor binding / carbohydrate transmembrane transporter activity / positive regulation of RNA polymerase II transcription preinitiation complex assembly / maltose binding / protein deubiquitination / blastocyst development / polyubiquitin modification-dependent protein binding / maltose transport / maltodextrin transmembrane transport / endopeptidase activator activity / proteasome assembly / mRNA export from nucleus / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / enzyme regulator activity / ERAD pathway / regulation of proteasomal protein catabolic process / inclusion body / ATP-binding cassette (ABC) transporter complex / proteasome complex / TBP-class protein binding / bioluminescence / stem cell differentiation / Regulation of activated PAK-2p34 by proteasome mediated degradation / cell chemotaxis / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / ubiquitin binding / generation of precursor metabolites and energy / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / P-body / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Degradation of DVL / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of CRY and PER proteins / Degradation of AXIN / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / G2/M Checkpoints / Hedgehog ligand biogenesis / Degradation of GLI1 by the proteasome / Defective CFTR causes cystic fibrosis / Autodegradation of the E3 ubiquitin ligase COP1 / Regulation of RUNX3 expression and activity / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / Hedgehog 'on' state / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Vif-mediated degradation of APOBEC3G / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Degradation of GLI2 by the proteasome Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() Homo sapiens (human) Purpureocillium lilacinum (fungus) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.65 Å | ||||||||||||||||||||||||
Authors | Zhu, C. / Qin, L. / Liang, L. | ||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural dynamics of the midnolin-proteasome during ubiquitin-independent substrate turnover Authors: Zhu, C. / Qin, L. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9w39.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9w39.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9w39.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w3/9w39 ftp://data.pdbj.org/pub/pdb/validation_reports/w3/9w39 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 65595MC ![]() 9mboC ![]() 9mbpC ![]() 9mbqC ![]() 9u3lC ![]() 9u4mC ![]() 9u7rC ![]() 9wbgC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 3 types, 3 molecules fec
| #1: Protein | Mass: 92188.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Homo sapiens (human)Gene: malE, b4034, JW3994, MIDN / Production host: ![]() |
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| #12: Protein | Mass: 8284.611 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P60896 |
| #15: Protein | Mass: 66145.211 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Purpureocillium lilacinum (fungus)Gene: PSMD14, POH1, PCL_01928 / Production host: ![]() References: UniProt: O00487, UniProt: A0A2U3DNX3, ubiquitinyl hydrolase 1 |
-26S proteasome regulatory subunit ... , 6 types, 6 molecules CDABEF
| #2: Protein | Mass: 45694.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62195 |
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| #3: Protein | Mass: 47426.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P43686 |
| #16: Protein | Mass: 48700.805 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P35998 |
| #17: Protein | Mass: 49260.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62191 |
| #18: Protein | Mass: 44241.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62333 |
| #19: Protein | Mass: 49266.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P17980 |
-26S proteasome non-ATPase regulatory subunit ... , 9 types, 9 molecules VWXYZabdU
| #4: Protein | Mass: 61066.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43242 |
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| #5: Protein | Mass: 52979.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O00232 |
| #6: Protein | Mass: 47526.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O00231 |
| #7: Protein | Mass: 45592.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15008 |
| #8: Protein | Mass: 37086.441 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P51665 |
| #9: Protein | Mass: 42995.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UNM6 |
| #10: Protein | Mass: 40781.590 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P55036 |
| #11: Protein | Mass: 39667.871 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P48556 |
| #14: Protein | Mass: 105958.234 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q99460 |
-Protein/peptide , 1 types, 1 molecules v
| #13: Protein/peptide | Mass: 613.749 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
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-Non-polymers , 4 types, 10 molecules 






| #20: Chemical | | #21: Chemical | ChemComp-ATP / #22: Chemical | ChemComp-ZN / | #23: Chemical | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.65 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 22385 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.65 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
Purpureocillium lilacinum (fungus)
China, 1items
Citation















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