Equivalence class NR_20.0_45472.4 Obsolete
# | IFE | Standardized name | Molecule | Organism | Source | Rfam | Title | Method | Res. Å | Date |
---|---|---|---|---|---|---|---|---|---|---|
1 | 6Q9A|1|4 (rep) | Transfer-messenger RNA | tmRNA | Escherichia coli | Bacteria | RF00023 | Structure of tmRNA SmpB bound past E site of E. coli 70S ribosome | Electron microscopy | 3.7 | 2019-04-17 |
2 | 6Q97|1|4 | Transfer-messenger RNA | transfer-messenger RNA (tmRNA) | Escherichia coli | Bacteria | RF00023 | Structure of tmRNA SmpB bound in A site of E. coli 70S ribosome | Electron microscopy | 3.9 | 2019-03-13 |
3 | 6Q98|1|4 | Transfer-messenger RNA | transfer-messenger RNA (tmRNA) | Escherichia coli | Bacteria | RF00023 | Structure of tmRNA SmpB bound in P site of E. coli 70S ribosome | Electron microscopy | 4.3 | 2019-02-27 |
4 | 3IZ4|1|A | Transfer-messenger RNA | Modified E. coli transfer-messenger RNA | Escherichia coli | Bacteria | RF00023 | Modified E. coli tmRNA in the resume state with the tRNA-like domain in the ribosomal P site interacting with the SmpB | Electron microscopy | 13.6 | 2010-10-20 |
5 | 4V6T|1|AV | Transfer-messenger RNA | full length transfer messenger RNA (tmRNA) | Escherichia coli | Bacteria | RF00023 | Structure of the bacterial ribosome complexed by tmRNA-SmpB and EF-G during translocation and MLD-loading | Electron microscopy | 8.3 | 2014-07-09 |
Release history
Release | 3.70 | 3.71 | 3.72 | 3.73 | 3.74 | 3.75 | 3.76 | 3.77 | 3.78 | 3.79 | 3.80 | 3.81 | 3.82 | 3.83 | 3.84 | 3.85 | 3.86 | 3.87 | 3.88 | 3.89 | 3.90 | 3.91 | 3.92 | 3.93 | 3.94 | 3.95 | 3.96 | 3.97 | 3.98 |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Date | 2019-04-19 | 2019-04-26 | 2019-05-03 | 2019-05-10 | 2019-05-17 | 2019-05-24 | 2019-05-31 | 2019-06-07 | 2019-06-14 | 2019-06-21 | 2019-06-28 | 2019-07-05 | 2019-07-12 | 2019-07-19 | 2019-07-26 | 2019-08-02 | 2019-08-09 | 2019-08-16 | 2019-08-23 | 2019-08-28 | 2019-09-04 | 2019-09-11 | 2019-09-19 | 2019-09-25 | 2019-10-03 | 2019-10-09 | 2019-10-16 | 2019-10-23 | 2019-10-30 |
Parents
Children
This class | Descendant classes | Release id | Intersection | Only in this class | Added to child |
---|---|---|---|---|---|
NR_20.0_45472.4 | NR_20.0_08930.1 | 3.99 | (1) 6Q9A|1|4 | (4) 3IZ4|1|A, 4V6T|1|AV, 6Q97|1|4, 6Q98|1|4 | (0) |
NR_20.0_45472.4 | NR_20.0_30521.1 | 3.99 | (2) 4V6T|1|AV, 6Q98|1|4 | (3) 3IZ4|1|A, 6Q97|1|4, 6Q9A|1|4 | (0) |
NR_20.0_45472.4 | NR_20.0_65254.1 | 3.99 | (1) 3IZ4|1|A | (4) 4V6T|1|AV, 6Q97|1|4, 6Q98|1|4, 6Q9A|1|4 | (0) |
NR_20.0_45472.4 | NR_20.0_82437.1 | 3.99 | (1) 6Q97|1|4 | (4) 3IZ4|1|A, 4V6T|1|AV, 6Q98|1|4, 6Q9A|1|4 | (0) |
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 | 3IZ4|1|A | Modified E. coli tmRNA in the resume state with the tRNA-like domain in the ribosomal P site interacting with the SmpB | ELECTRON MICROSCOPY | 13.6 | 377 | |
2 | 6Q98|1|4 | Structure of tmRNA SmpB bound in P site of E. coli 70S ribosome | ELECTRON MICROSCOPY | 4.3 | 363 | |
3 | 4V6T|1|AV | Structure of the bacterial ribosome complexed by tmRNA-SmpB and EF-G during translocation and MLD-loading | ELECTRON MICROSCOPY | 8.3 | 331 | |
4 | 6Q97|1|4 | Structure of tmRNA SmpB bound in A site of E. coli 70S ribosome | ELECTRON MICROSCOPY | 3.9 | 334 | |
5 | 6Q9A|1|4 | Structure of tmRNA SmpB bound past E site of E. coli 70S ribosome | ELECTRON MICROSCOPY | 3.7 | 363 |
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.
Coloring options: