+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9bji | ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Cryo-EM structure of apo NVL | ||||||||||||||||||||||||
Components |
| ||||||||||||||||||||||||
Keywords | TRANSLOCASE / Ribosome biogenesis / AAA+ ATPase | ||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of protein localization to nucleolus / preribosome binding / telomerase holoenzyme complex / telomerase holoenzyme complex assembly / positive regulation of telomere maintenance / positive regulation of protein binding / ribosomal large subunit biogenesis / rRNA processing / ribosome biogenesis / nucleolus ...regulation of protein localization to nucleolus / preribosome binding / telomerase holoenzyme complex / telomerase holoenzyme complex assembly / positive regulation of telomere maintenance / positive regulation of protein binding / ribosomal large subunit biogenesis / rRNA processing / ribosome biogenesis / nucleolus / ATP hydrolysis activity / RNA binding / nucleoplasm / ATP binding / nucleus / membrane Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.83 Å | ||||||||||||||||||||||||
Authors | Cruz, V.E. / Erzberger, J.P. | ||||||||||||||||||||||||
| Funding support | United States, 2items
| ||||||||||||||||||||||||
Citation | Journal: To Be PublishedTitle: Dibenzothiazepinones are bioavailable inhibitors of NVL and cause p53-dependent apoptosis in cancer by blocking 60S ribosome assembly Authors: Guo, H.H. / Tao, Y. / Cruz, V.E. / Fang, M. / Khivansara, V. / Xie, S. / Leach, A. / Rivera-Cancel, G. / Barrows, N. / Williams, N. / Aurora, A. / Erzberger, J.P. / De Brabander, J.K. / Nijhawan, D. | ||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9bji.cif.gz | 810.2 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9bji.ent.gz | 521.8 KB | Display | PDB format |
| PDBx/mmJSON format | 9bji.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9bji_validation.pdf.gz | 2.1 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 9bji_full_validation.pdf.gz | 2.1 MB | Display | |
| Data in XML | 9bji_validation.xml.gz | 93.2 KB | Display | |
| Data in CIF | 9bji_validation.cif.gz | 143.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bj/9bji ftp://data.pdbj.org/pub/pdb/validation_reports/bj/9bji | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 44633MC ![]() 9bjjC C: citing same article ( M: map data used to model this data |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
| #1: Protein/peptide | Mass: 3333.540 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Substrate mimic / Source: (gene. exp.) ![]() ![]() | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| #2: Protein | Mass: 95181.992 Da / Num. of mol.: 6 / Mutation: E365Q,E682Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NVL, NVL2 / Production host: ![]() #3: Chemical | ChemComp-ATP / #4: Chemical | ChemComp-MG / Has ligand of interest | Y | Has protein modification | N | |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: apo NVL / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: OTHER / Nominal defocus max: 1900 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 1.4 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-
Processing
| EM software | Name: PHENIX / Version: 1.21.1_5286 / Category: model refinement | ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.83 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 109860 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 38.66 Å2 | ||||||||||||||||||||||||
| Refine LS restraints |
|
Movie
Controller
About Yorodumi





Homo sapiens (human)
United States, 2items
Citation


PDBj






FIELD EMISSION GUN