Research workbench
Cryo-EM of elongating ribosome with EF-Tu*GTP elucidates tRNA proofreading (Cognate Structure IV-A)
Analyse Cryo-EM of elongating ribosome with EF-Tu*GTP elucidates tRNA proofreading… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WDB
- Type
- protein + RNA
- Length
- 10,830 residues
- Chains
- 58
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.0
- Source
- Escherichia coli; SYNTHETIC CONSTRUCT
- Molecule
- 50S ribosomal protein L2; 50S ribosomal protein L3; 50S ribosomal protein L4; 50S…
- UniProt
- P60422, P60438, P60723, P62399, P0AG55, P0A7R1, P0A7J3, P0A7J7, P0AA10, P0ADY3, P02413, P0ADY7, P0AG44, P0C018, P0A7K6, P0A7L3, P0AG48, P61175, P0ADZ0, P60624, P68919, P0A7L8, P0A7M2, P0A7M6, P0AG51, P0A7N4, P0A7N9, P0A7P5, P0A7Q1, P0A7Q6, P0A7V0, P0A7V3, P0A7V8, P0A7W1, P02358, P02359, P0A7W7, P0A7X3, P0A7R5, P0A7R9, P0A7S3, P0A7S9, P0AG59, P0ADZ4, P0A7T3, P0AG63, P0A7T7, P0A7U3, P0A7U7, P68679, P0A7L0
- Ligands
- FME
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · resolution 4.0 · 57 distinct chains · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| b | 50S ribosomal protein L2 | protein | 271 | 5% helix, 29% strand | P60422 |
| c | 50S ribosomal protein L3 | protein | 209 | 8% helix, 35% strand | P60438 |
| d | 50S ribosomal protein L4 | protein | 201 | 32% helix, 7% strand | P60723 |
| e | 50S ribosomal protein L5 | protein | 177 | 31% helix, 17% strand | P62399 |
| f | 50S ribosomal protein L6 | protein | 176 | 17% helix, 32% strand | P0AG55 |
| g | 50S ribosomal protein L9 | protein | 149 | 33% helix, 18% strand | P0A7R1 |
| h | 50S ribosomal protein L10 | protein | 131 | 34% helix, 2% strand | P0A7J3 |
| i | 50S ribosomal protein L11 | protein | 141 | 36% helix, 12% strand | P0A7J7 |
| j | 50S ribosomal protein L13 | protein | 142 | 26% helix, 15% strand | P0AA10 |
| k | 50S ribosomal protein L14 | protein | 122 | 7% helix, 34% strand | P0ADY3 |
| l | 50S ribosomal protein L15 | protein | 143 | 15% helix, 11% strand | P02413 |
| m | 50S ribosomal protein L16 | protein | 136 | 19% helix, 25% strand | P0ADY7 |
| n | 50S ribosomal protein L17 | protein | 120 | 43% helix, 18% strand | P0AG44 |
| o | 50S ribosomal protein L18 | protein | 116 | 41% helix, 16% strand | P0C018 |
| p | 50S ribosomal protein L19 | protein | 114 | 15% helix, 39% strand | P0A7K6 |
| q | 50S ribosomal protein L20 | protein | 117 | 74% helix, 0% strand | P0A7L3 |
| r | 50S ribosomal protein L21 | protein | 103 | 0% helix, 45% strand | P0AG48 |
| s | 50S ribosomal protein L22 | protein | 110 | 35% helix, 38% strand | P61175 |
| t | 50S ribosomal protein L23 | protein | 93 | 28% helix, 34% strand | P0ADZ0 |
| u | 50S ribosomal protein L24 | protein | 102 | 0% helix, 39% strand | P60624 |
| v | 50S ribosomal protein L25 | protein | 94 | 20% helix, 41% strand | P68919 |
| w | 50S ribosomal protein L27 | protein | 75 | 0% helix, 37% strand | P0A7L8 |
| x | 50S ribosomal protein L28 | protein | 77 | 26% helix, 31% strand | P0A7M2 |
| y | 50S ribosomal protein L29 | protein | 63 | 70% helix, 0% strand | P0A7M6 |
| z | 50S ribosomal protein L30 | protein | 58 | 29% helix, 26% strand | P0AG51 |
| B | 50S ribosomal protein L32 | protein | 56 | 13% helix, 11% strand | P0A7N4 |
| C | 50S ribosomal protein L33 | protein | 50 | 0% helix, 32% strand | P0A7N9 |
| D | 50S ribosomal protein L34 | protein | 46 | 50% helix, 0% strand | P0A7P5 |
| E | 50S ribosomal protein L35 | protein | 64 | 27% helix, 13% strand | P0A7Q1 |
| F | 50S ribosomal protein L36 | protein | 38 | 16% helix, 8% strand | P0A7Q6 |
| G | 30S ribosomal protein S2 | protein | 225 | 49% helix, 14% strand | P0A7V0 |
| H | 30S ribosomal protein S3 | protein | 206 | 37% helix, 30% strand | P0A7V3 |
| I | 30S ribosomal protein S4 | protein | 205 | 39% helix, 6% strand | P0A7V8 |
| J | 30S ribosomal protein S5 | protein | 157 | 25% helix, 25% strand | P0A7W1 |
| K | 30S ribosomal protein S6 | protein | 100 | 31% helix, 23% strand | P02358 |
| L | 30S ribosomal protein S7 | protein | 151 | 54% helix, 5% strand | P02359 |
| M | 30S ribosomal protein S8 | protein | 129 | 28% helix, 29% strand | P0A7W7 |
| N | 30S ribosomal protein S9 | protein | 127 | 25% helix, 17% strand | P0A7X3 |
| O | 30S ribosomal protein S10 | protein | 98 | 23% helix, 36% strand | P0A7R5 |
| P | 30S ribosomal protein S11 | protein | 116 | 18% helix, 26% strand | P0A7R9 |
| Q | 30S ribosomal protein S12 | protein | 123 | 5% helix, 21% strand | P0A7S3 |
| R | 30S ribosomal protein S13 | protein | 114 | 48% helix, 2% strand | P0A7S9 |
| S | 30S ribosomal protein S14 | protein | 100 | 40% helix, 7% strand | P0AG59 |
| T | 30S ribosomal protein S15 | protein | 88 | 72% helix, 0% strand | P0ADZ4 |
| U | 30S ribosomal protein S16 | protein | 82 | 21% helix, 23% strand | P0A7T3 |
| V | 30S ribosomal protein S17 | protein | 80 | 0% helix, 39% strand | P0AG63 |
| W | 30S ribosomal protein S18 | protein | 65 | 42% helix, 3% strand | P0A7T7 |
| X | 30S ribosomal protein S19 | protein | 79 | 23% helix, 13% strand | P0A7U3 |
| Y | 30S ribosomal protein S20 | protein | 85 | 86% helix, 0% strand | P0A7U7 |
| Z | 30S ribosomal protein S21 | protein | 65 | 40% helix, 3% strand | P68679 |
| a | 50S ribosomal protein L1 | protein | 134 | 28% helix, 28% strand | P0A7L0 |
| 3 | 16S ribosomal RNA | rna | 1539 | — | — |
| 1 | 23S ribosomal RNA | rna | 2903 | — | — |
| 2 | 5S ribosomal RNA | rna | 120 | — | — |
| 5, 6 | tRNAfMet | rna | 77 | — | — |
| 4 | mRNA | rna | 18 | — | — |
| 7 | tRNAPhe | rna | 73 | — | — |
Ligands and binding sites
- FME · N-formylmethionine · ligand · chains 1, 5
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1013 | 0.89 | 0.91 | 117 | empty |
| 2 | 1157 | 0.88 | 0.91 | 143 | empty |
| 3 | 1022 | 0.88 | 0.90 | 88 | FME |
| 4 | 1107 | 0.88 | 0.90 | 108 | empty |
| 5 | 1073 | 0.87 | 0.89 | 88 | empty |
Interfaces
142 interfaces between chains.
- b–1 · 7473 Ų buried · 172 hydrogen bonds · protein-nucleic
- c–1 · 5248 Ų buried · 126 hydrogen bonds · protein-nucleic
- l–1 · 4605 Ų buried · 107 hydrogen bonds · protein-nucleic
- d–1 · 4369 Ų buried · 85 hydrogen bonds · protein-nucleic
- q–1 · 4226 Ų buried · 95 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- P0A7L0 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L1 (P0A7L0) · a predicted model of the same protein · chain a against A, TM-score 0.95
- P0A7J3 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L10 (P0A7J3) · a predicted model of the same protein · chain h against A, TM-score 0.81
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P60422
- Every structure of UniProt P60438
- Every structure of UniProt P60723
- Every structure of UniProt P62399
- Every structure of UniProt P0AG55
- Every structure of UniProt P0A7R1
- Every structure of UniProt P0A7J3
- Every structure of UniProt P0A7J7
- Every structure of UniProt P0AA10
- Every structure of UniProt P0ADY3
- Every structure of UniProt P02413
- Every structure of UniProt P0ADY7
- Every structure of UniProt P0AG44
- Every structure of UniProt P0C018
- Every structure of UniProt P0A7K6
- Every structure of UniProt P0A7L3
- Every structure of UniProt P0AG48
- Every structure of UniProt P61175
- Every structure of UniProt P0ADZ0
- Every structure of UniProt P60624
- Every structure of UniProt P68919
- Every structure of UniProt P0A7L8
- Every structure of UniProt P0A7M2
- Every structure of UniProt P0A7M6
- Every structure of UniProt P0AG51
- Every structure of UniProt P0A7N4
- Every structure of UniProt P0A7N9
- Every structure of UniProt P0A7P5
- Every structure of UniProt P0A7Q1
- Every structure of UniProt P0A7Q6
- Every structure of UniProt P0A7V0
- Every structure of UniProt P0A7V3
- Every structure of UniProt P0A7V8
- Every structure of UniProt P0A7W1
- Every structure of UniProt P02358
- Every structure of UniProt P02359
- Every structure of UniProt P0A7W7
- Every structure of UniProt P0A7X3
- Every structure of UniProt P0A7R5
- Every structure of UniProt P0A7R9
- Every structure of UniProt P0A7S3
- Every structure of UniProt P0A7S9
- Every structure of UniProt P0AG59
- Every structure of UniProt P0ADZ4
- Every structure of UniProt P0A7T3
- Every structure of UniProt P0AG63
- Every structure of UniProt P0A7T7
- Every structure of UniProt P0A7U3
- Every structure of UniProt P0A7U7
- Every structure of UniProt P68679
- Every structure of UniProt P0A7L0
- Elsewhere: RCSB PDB 6WDB · PDBe 6WDB · UniProt P60422 · UniProt P60438 · UniProt P60723 · UniProt P62399 · UniProt P0AG55 · UniProt P0A7R1 · UniProt P0A7J3 · UniProt P0A7J7 · UniProt P0AA10 · UniProt P0ADY3 · UniProt P02413 · UniProt P0ADY7 · UniProt P0AG44 · UniProt P0C018 · UniProt P0A7K6 · UniProt P0A7L3 · UniProt P0AG48 · UniProt P61175 · UniProt P0ADZ0 · UniProt P60624 · UniProt P68919 · UniProt P0A7L8 · UniProt P0A7M2 · UniProt P0A7M6 · UniProt P0AG51 · UniProt P0A7N4 · UniProt P0A7N9 · UniProt P0A7P5 · UniProt P0A7Q1 · UniProt P0A7Q6 · UniProt P0A7V0 · UniProt P0A7V3 · UniProt P0A7V8 · UniProt P0A7W1 · UniProt P02358 · UniProt P02359 · UniProt P0A7W7 · UniProt P0A7X3 · UniProt P0A7R5 · UniProt P0A7R9 · UniProt P0A7S3 · UniProt P0A7S9 · UniProt P0AG59 · UniProt P0ADZ4 · UniProt P0A7T3 · UniProt P0AG63 · UniProt P0A7T7 · UniProt P0A7U3 · UniProt P0A7U7 · UniProt P68679 · UniProt P0A7L0
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