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Open data
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Basic information
| Entry | Database: PDB / ID: 9ojm | ||||||||||||||||||||||||
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| Title | Human mitochondrial 28S PIC with tRNA and mtIF2 | ||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / Mitochondrial Ribosome 28S pre-initiation complex | ||||||||||||||||||||||||
| Function / homology | Function and homology informationmitochondrial translational initiation / translation factor activity, RNA binding / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / negative regulation of mitotic nuclear division / mitochondrial ribosome / ribosome disassembly ...mitochondrial translational initiation / translation factor activity, RNA binding / mitochondrial ribosome assembly / Mitochondrial translation elongation / Mitochondrial translation initiation / Mitochondrial ribosome-associated quality control / Mitochondrial translation termination / negative regulation of mitotic nuclear division / mitochondrial ribosome / ribosome disassembly / mitochondrial small ribosomal subunit / regulation of translational initiation / mitochondrial translation / positive regulation of proteolysis / apoptotic mitochondrial changes / ribosomal small subunit binding / translation initiation factor activity / Mitochondrial protein degradation / apoptotic signaling pathway / fibrillar center / regulation of translation / small ribosomal subunit / small ribosomal subunit rRNA binding / nuclear membrane / intracellular membrane-bounded organelle / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / tRNA binding / cell population proliferation / mitochondrial inner membrane / rRNA binding / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / GTPase activity / mRNA binding / GTP binding / nucleolus / mitochondrion / RNA binding / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.5 Å | ||||||||||||||||||||||||
Authors | Kober, D.L. / Wang, J. | ||||||||||||||||||||||||
| Funding support | United States, 4items
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Citation | Journal: Nat Commun / Year: 2026Title: Mechanisms of human mitochondrial leaderless mRNA translation initiation Authors: Shen, S. / Xu, Y. / Kober, D.L. / Wang, J. | ||||||||||||||||||||||||
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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 | 9ojm.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ojm.ent.gz | 1.4 MB | Display | PDB format |
| PDBx/mmJSON format | 9ojm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oj/9ojm ftp://data.pdbj.org/pub/pdb/validation_reports/oj/9ojm | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 70544MC C: citing same article ( M: map data used to model this data |
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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
-Small ribosomal subunit protein ... , 18 types, 18 molecules 0134BGHILMNRTUVWXZ
| #1: Protein | Mass: 25336.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82930 |
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| #2: Protein | Mass: 32156.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82673 |
| #4: Protein | Mass: 8936.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NWT8 |
| #5: Protein | Mass: 70984.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EY7 |
| #10: Protein | Mass: 25988.881 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y399 |
| #15: Protein | Mass: 40136.102 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82933 |
| #16: Protein | Mass: 16360.981 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82664 |
| #17: Protein | Mass: 14509.841 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82912 |
| #20: Protein | Mass: 20729.482 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82914 |
| #21: Protein | Mass: 13438.712 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y3D3 |
| #22: Protein | Mass: 12349.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2R5 |
| #26: Protein | Mass: 34251.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82650 |
| #28: Protein | Mass: 19585.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82663 |
| #29: Protein | Mass: 21183.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BYN8 |
| #30: Protein | Mass: 43969.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q92552 |
| #31: Protein | Mass: 11263.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2Q9 |
| #32: Protein | Mass: 40421.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P51398, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
| #34: Protein | Mass: 11952.871 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y291 |
-Protein , 2 types, 2 molecules 27
| #3: Protein | Mass: 13498.819 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96BP2 |
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| #8: Protein | Mass: 63169.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P46199 |
-RNA chain , 3 types, 3 molecules 56A
| #6: RNA chain | Mass: 22664.498 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: GenBank: 1896813686 |
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| #7: RNA chain | Mass: 1241.786 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
| #9: RNA chain | Mass: 306547.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 1858621102 |
-28S ribosomal protein ... , 11 types, 11 molecules CDEFJKOPQSY
| #11: Protein | Mass: 15333.757 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96EL2 |
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| #12: Protein | Mass: 38919.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82675 |
| #13: Protein | Mass: 13861.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82932 |
| #14: Protein | Mass: 24569.783 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2R9 |
| #18: Protein | Mass: 12013.163 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15235 |
| #19: Protein | Mass: 12282.349 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60783 |
| #23: Protein | Mass: 22573.775 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #24: Protein | Mass: 11188.229 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #25: Protein | Mass: 10764.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P82921 |
| #27: Protein | Mass: 15702.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #33: Protein | Mass: 17631.842 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
-Non-polymers , 8 types, 1497 molecules 














| #35: Chemical | ChemComp-MG / #36: Chemical | ChemComp-K / #37: Chemical | ChemComp-GTP / | #38: Chemical | ChemComp-ZN / | #39: Chemical | #40: Chemical | ChemComp-GDP / | #41: Chemical | ChemComp-ATP / | #42: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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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
| Component | Name: Human mitochondrial 28S PIC with tRNA and mtIF2 / Type: RIBOSOME / Entity ID: #1-#34 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| 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: 2500 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3D reconstruction | Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 107666 / Symmetry type: POINT | ||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT |
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About Yorodumi




Homo sapiens (human)
United States, 4items
Citation

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FIELD EMISSION GUN