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Open data
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Basic information
| Entry | Database: PDB / ID: 9iax | ||||||||||||||||||||||||
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| Title | DNA-PK, LX4, XLF - Catalytic domain of L4 | ||||||||||||||||||||||||
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Keywords | DNA BINDING PROTEIN / Kinase / NHEJ / cryo-EM / DNA-PK | ||||||||||||||||||||||||
| Function / homology | Function and homology informationFHA domain binding / positive regulation of chromosome organization / positive regulation of ligase activity / DNA ligase IV complex / DNA ligase activity / positive regulation of platelet formation / DN2 thymocyte differentiation / DNA double-strand break attachment to nuclear envelope / DNA ligase (ATP) / Ku70:Ku80 complex ...FHA domain binding / positive regulation of chromosome organization / positive regulation of ligase activity / DNA ligase IV complex / DNA ligase activity / positive regulation of platelet formation / DN2 thymocyte differentiation / DNA double-strand break attachment to nuclear envelope / DNA ligase (ATP) / Ku70:Ku80 complex / T cell receptor V(D)J recombination / negative regulation of t-circle formation / pro-B cell differentiation / DNA end binding / DNA ligase (ATP) activity / DNA-dependent protein kinase activity / small-subunit processome assembly / positive regulation of lymphocyte differentiation / histone H2AXS139 kinase activity / DNA-dependent protein kinase complex / DNA-dependent protein kinase-DNA ligase 4 complex / immunoglobulin V(D)J recombination / nonhomologous end joining complex / nucleotide-excision repair, DNA gap filling / single strand break repair / immature B cell differentiation / V(D)J recombination / regulation of smooth muscle cell proliferation / cellular response to X-ray / regulation of epithelial cell proliferation / double-strand break repair via alternative nonhomologous end joining / double-strand break repair via classical nonhomologous end joining / isotype switching / nuclear telomere cap complex / Cytosolic sensors of pathogen-associated DNA / protein localization to site of double-strand break / telomere capping / IRF3-mediated induction of type I IFN / regulation of hematopoietic stem cell differentiation / recombinational repair / regulation of telomere maintenance / positive regulation of neurogenesis / U3 snoRNA binding / DNA biosynthetic process / protein localization to chromosome, telomeric region / T cell lineage commitment / maturation of 5.8S rRNA / cellular response to lithium ion / cellular hyperosmotic salinity response / positive regulation of double-strand break repair via nonhomologous end joining / B cell lineage commitment / negative regulation of cGAS/STING signaling pathway / 2-LTR circle formation / response to ionizing radiation / hematopoietic stem cell proliferation / peptidyl-threonine phosphorylation / ligase activity / telomeric DNA binding / DNA 3'-5' helicase / negative regulation of protein phosphorylation / positive regulation of protein kinase activity / T cell differentiation / somatic stem cell population maintenance / 5'-deoxyribose-5-phosphate lyase activity / hematopoietic stem cell differentiation / chromosome organization / response to X-ray / somitogenesis / ATP-dependent activity, acting on DNA / ectopic germ cell programmed cell death / site of DNA damage / telomere maintenance via telomerase / SUMOylation of DNA damage response and repair proteins / condensed chromosome / mitotic G1 DNA damage checkpoint signaling / DNA polymerase binding / neurogenesis / activation of innate immune response / positive regulation of erythrocyte differentiation / DNA helicase activity / B cell differentiation / telomere maintenance / cyclin binding / central nervous system development / stem cell proliferation / DNA-(apurinic or apyrimidinic site) lyase / positive regulation of translation / cellular response to leukemia inhibitory factor / cellular response to ionizing radiation / response to gamma radiation / protein modification process / Nonhomologous End-Joining (NHEJ) / small-subunit processome / peptidyl-serine phosphorylation / enzyme activator activity / protein-DNA complex / cellular response to gamma radiation / regulation of circadian rhythm / brain development / base-excision repair Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human)DNA molecule (others) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.97 Å | ||||||||||||||||||||||||
Authors | Chaplin, A.K. / Hall, C. | ||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: To Be PublishedTitle: New insight into how the DNA binding domain of DNA ligase IV facilitates end-joining, independent of its catalytic activity. Authors: Chaplin, A.K. / Hall, C. | ||||||||||||||||||||||||
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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 | 9iax.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9iax.ent.gz | 921.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9iax.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ia/9iax ftp://data.pdbj.org/pub/pdb/validation_reports/ia/9iax | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52786MC 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 , 4 types, 6 molecules ADMGHK
| #1: Protein | Mass: 469673.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P78527, non-specific serine/threonine protein kinase | ||||
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| #4: Protein | Mass: 33372.234 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NHEJ1, XLF / Production host: ![]() #5: Protein | Mass: 38337.703 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: XRCC4 / Production host: ![]() #6: Protein | | Mass: 104124.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LIG4 / Production host: ![]() |
-X-ray repair cross-complementing protein ... , 2 types, 2 molecules BC
| #2: Protein | Mass: 69945.039 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: XRCC6, G22P1 / Production host: ![]() References: UniProt: P12956, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement, Lyases; Carbon-oxygen lyases; Other carbon-oxygen lyases |
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| #3: 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, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
-DNA chain , 2 types, 2 molecules de
| #7: DNA chain | Mass: 16799.797 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) DNA molecule (others) |
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| #8: DNA chain | Mass: 13007.345 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) DNA molecule (others) |
-Details
| Has protein modification | N |
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-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
| Component | Name: DNA-PK, LX4, XLF complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.2 |
| 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: DARK FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 49.6 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487 / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.97 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 6996 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.97 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
United Kingdom, 1items
Citation
PDBj
















































FIELD EMISSION GUN