Equivalence class NR_4.0_97435.2 Obsolete
# | IFE | Compound(s) | RNA source organism | Title | Method | Resolution | Date |
---|---|---|---|---|---|---|---|
1 | 6HA1|1|B (rep) | 5S ribosomal RNA | Bacillus subtilis | Cryo-EM structure of a 70S Bacillus subtilis ribosome translating the ErmD leader peptide in complex with telithromycin | ELECTRON MICROSCOPY | 3.1 | 2018-08-29 |
2 | 6HA8|1|B | 5S rRNA | Bacillus subtilis | Cryo-EM structure of the ABCF protein VmlR bound to the Bacillus subtilis ribosome | ELECTRON MICROSCOPY | 3.5 | 2018-08-29 |
3 | 6PPF|1|B | 5S rRNA | Bacillus subtilis | Bacterial 45SRbgA ribosomal particle class B | ELECTRON MICROSCOPY | 3.4 | 2019-09-18 |
4 | 5NJT|1|V | 5S ribosomal RNA | Bacillus subtilis | Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization. | ELECTRON MICROSCOPY | 3.8 | 2017-06-14 |
5 | 3J9W|1|BB | 5S ribosomal RNA | Bacillus subtilis | Cryo-EM structure of the Bacillus subtilis MifM-stalled ribosome complex | ELECTRON MICROSCOPY | 3.9 | 2015-04-29 |
Parents
Heat map of mutual geometric discrepancy, in Angstroms per nucleotide. Instances are ordered to put similar structures near each other. The colorbar ranges from 0 to the maximum observed discrepancy, up to 0.5
#S - ordering by similarity (same as in the heat map).#S | PDB | Title | Method | Resolution | Length |
---|---|---|---|---|---|
1 | 6HA1|1|B | Cryo-EM structure of a 70S Bacillus subtilis ribosome translating the ErmD leader peptide in complex with telithromycin | ELECTRON MICROSCOPY | 3.1 | 112 |
2 | 6HA8|1|B | Cryo-EM structure of the ABCF protein VmlR bound to the Bacillus subtilis ribosome | ELECTRON MICROSCOPY | 3.5 | 112 |
3 | 5NJT|1|V | Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization. | ELECTRON MICROSCOPY | 3.8 | 112 |
4 | 3J9W|1|BB | Cryo-EM structure of the Bacillus subtilis MifM-stalled ribosome complex | ELECTRON MICROSCOPY | 3.9 | 112 |
5 | 6PPF|1|B | Bacterial 45SRbgA ribosomal particle class B | ELECTRON MICROSCOPY | 3.4 | 112 |