+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9znc | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | CryoEM structure of the DNA-PK complex bound to N20 nucleosome | |||||||||
Components |
| |||||||||
Keywords | DNA BINDING PROTEIN/DNA / NHEJ / DNA-PK / DNA repair / nucleosome / Ku70/80 / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex | |||||||||
| Function / homology | Function and homology informationpositive regulation of platelet formation / Ku70:Ku80 complex / negative regulation of t-circle formation / DNA-dependent protein kinase activity / DNA end binding / small-subunit processome assembly / positive regulation of lymphocyte differentiation / DNA-dependent protein kinase complex / DNA-dependent protein kinase-DNA ligase 4 complex / immunoglobulin V(D)J recombination ...positive regulation of platelet formation / Ku70:Ku80 complex / negative regulation of t-circle formation / DNA-dependent protein kinase activity / DNA end binding / small-subunit processome assembly / positive regulation of lymphocyte differentiation / DNA-dependent protein kinase complex / DNA-dependent protein kinase-DNA ligase 4 complex / immunoglobulin V(D)J recombination / histone H2AXS139 kinase activity / nonhomologous end joining complex / cellular response to X-ray / regulation of epithelial cell proliferation / regulation of smooth muscle cell proliferation / double-strand break repair via classical nonhomologous end joining / double-strand break repair via alternative nonhomologous end joining / Cytosolic sensors of pathogen-associated DNA / nuclear telomere cap complex / telomere capping / IRF3-mediated induction of type I IFN / regulation of hematopoietic stem cell differentiation / cellular hyperosmotic salinity response / U3 snoRNA binding / regulation of telomere maintenance / recombinational repair / maturation of 5.8S rRNA / protein localization to chromosome, telomeric region / positive regulation of double-strand break repair via nonhomologous end joining / negative regulation of cGAS/STING signaling pathway / 2-LTR circle formation / peptidyl-threonine phosphorylation / telomeric repeat DNA binding / negative regulation of protein phosphorylation / DNA 3'-5' helicase / 5'-deoxyribose-5-phosphate lyase activity / ATP-dependent activity, acting on DNA / 3'-5' DNA helicase activity / telomere maintenance via telomerase / mitotic G1 DNA damage checkpoint signaling / positive regulation of erythrocyte differentiation / activation of innate immune response / telomere maintenance / cyclin binding / protein modification process / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / DNA helicase activity / site of DNA damage / intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of translation / small-subunit processome / Nonhomologous End-Joining (NHEJ) / cellular response to gamma radiation / protein-DNA complex / peptidyl-serine phosphorylation / double-strand break repair via nonhomologous end joining / regulation of circadian rhythm / enzyme activator activity / nucleosomal DNA binding / innate immune response in mucosa / double-strand break repair / structural constituent of chromatin / cellular response to insulin stimulus / nucleosome / nucleosome assembly / E3 ubiquitin ligases ubiquitinate target proteins / transcription regulator complex / chromatin organization / DNA recombination / antimicrobial humoral immune response mediated by antimicrobial peptide / double-stranded DNA binding / heterochromatin formation / scaffold protein binding / secretory granule lumen / antibacterial humoral response / ficolin-1-rich granule lumen / damaged DNA binding / RNA polymerase II-specific DNA-binding transcription factor binding / protein kinase activity / innate immune response / protein phosphorylation / chromosome, telomeric region / non-specific serine/threonine protein kinase / transcription cis-regulatory region binding / chromosome / ribonucleoprotein complex / protein heterodimerization activity / protein domain specific binding / protein serine kinase activity / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / protein serine/threonine kinase activity / DNA damage response / negative regulation of apoptotic process / nucleolus / Neutrophil degranulation / positive regulation of DNA-templated transcription / chromatin / protein-containing complex binding Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.93 Å | |||||||||
Authors | Lu, W. / He, Y. | |||||||||
| Funding support | United States, 1items
| |||||||||
Citation | Journal: Nat Commun / Year: 2026Title: DNA-PK driven nucleosome unwrapping enables NHEJ in chromatin Authors: Lu, W. / Vogt, A. / Lees-Miller, S.P. / He, Y. | |||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9znc.cif.gz | 2 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9znc.ent.gz | 1.7 MB | Display | PDB format |
| PDBx/mmJSON format | 9znc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zn/9znc ftp://data.pdbj.org/pub/pdb/validation_reports/zn/9znc | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 74444MC ![]() 9zmmC ![]() 9zobC ![]() 9zp0C ![]() 9zp9C 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
-Protein , 7 types, 11 molecules AEBFCGDHMKL
| #1: Protein | Mass: 12830.009 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Protein | Mass: 9990.770 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #3: Protein | Mass: 12740.877 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #4: Protein | Mass: 11179.959 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #6: Protein | | Mass: 469673.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P78527#9: Protein | | Mass: 69945.039 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() #10: Protein | | Mass: 82812.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: XRCC5, G22P2 / Production host: ![]() References: UniProt: P13010, DNA-(apurinic or apyrimidinic site) lyase, DNA 3'-5' helicase |
|---|
-DNA chain , 2 types, 2 molecules IJ
| #5: DNA chain | Mass: 50923.418 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
|---|---|
| #8: DNA chain | Mass: 50332.059 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
-Protein/peptide , 1 types, 1 molecules N
| #7: Protein/peptide | Mass: 1720.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
|---|
-Details
| 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 |
| ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Molecular weight |
| ||||||||||||||||||||||||
| Source (natural) |
| ||||||||||||||||||||||||
| Source (recombinant) |
| ||||||||||||||||||||||||
| Buffer solution | pH: 7 | ||||||||||||||||||||||||
| 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: BRIGHT FIELD / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm |
| Image recording | Electron dose: 62 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
-
Processing
| EM software |
| ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||
| 3D reconstruction | Resolution: 3.93 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 68925 / Symmetry type: POINT |
Movie
Controller
About Yorodumi




Homo sapiens (human)
United States, 1items
Citation























PDBj















































FIELD EMISSION GUN