Equivalence class NR_3.5_56101.2 Obsolete
| # | IFE | Standardized name | Molecule | Organism | Source | Rfam | Title | Method | Res. Å | Date |
|---|---|---|---|---|---|---|---|---|---|---|
| 1 | 7O1A|1|B8 (rep) | Transfer RNA | mRNA, P-site tRNA-Pro | Escherichia coli K-12 | Bacteria | RF00005 | Cryo-EM structure of an Escherichia coli TnaC(R23F)-ribosome complex stalled in response to L-tryptophan | Electron microscopy | 2.4 | 2021-09-01 |
| 2 | 7O1C|1|B8 | Transfer RNA | mRNA, P-site tRNA-Pro | Escherichia coli K-12 | Bacteria | RF00005 | Cryo-EM structure of an Escherichia coli TnaC(R23F)-ribosome-RF2 complex stalled in response to L-tryptophan | Electron microscopy | 2.6 | 2021-09-01 |
| 3 | 7O19|1|B8 | Transfer RNA | mRNA, P-site tRNA-Pro | Escherichia coli K-12 | Bacteria | RF00005 | Cryo-EM structure of an Escherichia coli TnaC-ribosome complex stalled in response to L-tryptophan | Electron microscopy | 2.9 | 2021-09-01 |
| 4 | 6SZS|1|x | Transfer RNA | mRNA, P-site tRNA-Pro(CGG) | Escherichia coli | Bacteria | RF00005 | Release factor-dependent ribosome rescue by BrfA in the Gram-positive bacterium Bacillus subtilis | Electron microscopy | 3.06 | 2019-12-04 |
| 5 | 5MGP|1|x | Transfer RNA | mRNA, P-site tRNA | Escherichia coli | Bacteria | RF00005 | Structural basis for ArfA-RF2 mediated translation termination on stop-codon lacking mRNAs | Electron microscopy | 3.1 | 2016-12-14 |
| 6 | 6ENU|1|x | Transfer RNA | mRNA, Proline tRNA | Escherichia coli | Bacteria | RF00005 | Polyproline-stalled ribosome in the presence of elongation-factor P (EF-P) | Electron microscopy | 3.1 | 2017-11-22 |
| 7 | 6ENF|1|x | Transfer RNA | proline tRNA, RNA (5'-R(P*CP*CP*G)-3'), mRNA | Escherichia coli | Bacteria | RF00005 | Cryo-EM structure of a polyproline-stalled ribosome in the absence of EF-P | Electron microscopy | 3.2 | 2017-11-22 |
| 8 | 6NUO|1|XV | Transfer RNA | mRNA, P-site tRNA-Pro | Escherichia coli | Bacteria | RF00005 | Modified tRNA(Pro) bound to Thermus thermophilus 70S (cognate) | X-ray diffraction | 3.2 | 2020-10-14 |
| 9 | 6NUO|1|QV | Transfer RNA | mRNA, P-site tRNA-Pro | Escherichia coli | Bacteria | RF00005 | Modified tRNA(Pro) bound to Thermus thermophilus 70S (cognate) | X-ray diffraction | 3.2 | 2020-10-14 |
Release history
Parents
Instances are ordered to put similar structures near each other. Select one instance to see its 3D structure. Selecting two or more instances will show their superposition, but only chains with identical numbers of observed nucleotides will superpose well. Large structures are slow to display; this tool is not designed for that.
| #S | View | PDB | Title | Method | Resolution | Length |
|---|---|---|---|---|---|---|
| 1 | 6ENF|1|x | Cryo-EM structure of a polyproline-stalled ribosome in the absence of EF-P | ELECTRON MICROSCOPY | 3.2 | 77 | |
| 2 | 6ENU|1|x | Polyproline-stalled ribosome in the presence of elongation-factor P (EF-P) | ELECTRON MICROSCOPY | 3.1 | 77 | |
| 3 | 7O19|1|B8 | Cryo-EM structure of an Escherichia coli TnaC-ribosome complex stalled in response to L-tryptophan | ELECTRON MICROSCOPY | 2.9 | 77 | |
| 4 | 7O1C|1|B8 | Cryo-EM structure of an Escherichia coli TnaC(R23F)-ribosome-RF2 complex stalled in response to L-tryptophan | ELECTRON MICROSCOPY | 2.6 | 77 | |
| 5 | 7O1A|1|B8 | Cryo-EM structure of an Escherichia coli TnaC(R23F)-ribosome complex stalled in response to L-tryptophan | ELECTRON MICROSCOPY | 2.4 | 74 | |
| 6 | 5MGP|1|x | Structural basis for ArfA-RF2 mediated translation termination on stop-codon lacking mRNAs | ELECTRON MICROSCOPY | 3.1 | 77 | |
| 7 | 6SZS|1|x | Release factor-dependent ribosome rescue by BrfA in the Gram-positive bacterium Bacillus subtilis | ELECTRON MICROSCOPY | 3.06 | 77 | |
| 8 | 6NUO|1|XV | Modified tRNA(Pro) bound to Thermus thermophilus 70S (cognate) | X-RAY DIFFRACTION | 3.2 | 76 | |
| 9 | 6NUO|1|QV | Modified tRNA(Pro) bound to Thermus thermophilus 70S (cognate) | X-RAY DIFFRACTION | 3.2 | 76 |
Heat map of mutual geometric discrepancy, in Angstroms per nucleotide. The ordering in the heat map is the same as in the table. The colorbar ranges from 0 to the maximum observed discrepancy. Click above the diagonal to select a range of structures, below the diagonal to select two structures.
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