Equivalence class NR_3.0_56101.2 Obsolete
| # | IFE | Standardized name | Molecule | Organism | Source | Rfam | Title | Method | Å | Date |
|---|---|---|---|---|---|---|---|---|---|---|
| 1 | 7O1A|1|B8 (rep) | Transfer RNA | P-site tRNA-Pro, mRNA | 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 | P-site tRNA-Pro, mRNA | 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 | P-site tRNA-Pro, mRNA | 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 |
Release history
Parents
| This class | Parent classes | Release id | Intersection | Added to this class | Only in parent |
|---|
Children
| This class | Descendant classes | Release id | Intersection | Only in this class | Added to child |
|---|---|---|---|---|---|
| NR_3.0_56101.2 | NR_3.0_56101.3 | 3.208 | (3) 7O19|1|B8, 7O1A|1|B8, 7O1C|1|B8 | (0) | (0) |
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 | 7O19|1|B8 | Cryo-EM structure of an Escherichia coli TnaC-ribosome complex stalled in response to L-tryptophan | ELECTRON MICROSCOPY | 2.9 | 77 |
| 2 | 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 |
| 3 | 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 |