70S Escherichia coli ribosome with Paenilamicin B2 bound with A- and P-site tRNA. Determined by electron microscopy at 2.2 Å resolution. Released 24 Jul 2024.
Explore 8R6C in 3D Show helices and sheets RCSB PDB PDBe
8R6C contains 262 α-helices and 306 β-strands across 50 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6 | 1 | |
| β-strand | 7-13 | 7 | 1 |
| β-strand | 20-25 | 6 | 1 |
| α-helix | 33-34 | 2 | |
| β-strand | 35-40 | 6 | 1 |
| β-strand | 45-53 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-16 | 8 | |
| α-helix | 18-22 | 5 | |
| α-helix | 25-37 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-11 | 4 | |
| β-strand | 15-16 | 2 | 4 |
| β-strand | 22-24 | 3 | 4 |
| α-helix | 25-26 | 2 | |
| α-helix | 38-44 | 7 | |
| β-strand | 48-49 | 2 | 4 |
| α-helix | 50-51 | 2 | |
| α-helix | 52-61 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 6 |
| β-strand | 14-18 | 5 | 6 |
| β-strand | 23-27 | 5 | 6 |
| α-helix | 31-33 | 3 | |
| β-strand | 35-37 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-8 | 2 | |
| β-strand | 10-13 | 4 | 9 |
| β-strand | 14-16 | 3 | 10 |
| β-strand | 23-26 | 4 | 9 |
| β-strand | 32-34 | 3 | 10 |
| α-helix | 42-45 | 4 | |
| α-helix | 56-64 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-12 | 7 | |
| β-strand | 16-19 | 4 | 20 |
| α-helix | 20-22 | 3 | |
| α-helix | 25-30 | 6 | |
| β-strand | 31-34 | 4 | 20 |
| β-strand | 38-41 | 4 | 20 |
| α-helix | 43-62 | 20 | |
| β-strand | 67-70 | 4 | 21 |
| α-helix | 76-86 | 11 | |
| β-strand | 90-92 | 3 | 21 |
| α-helix | 96-97 | 2 | |
| α-helix | 104-123 | 20 | |
| α-helix | 132-148 | 17 | |
| β-strand | 160-164 | 5 | 21 |
| α-helix | 170-178 | 9 | |
| β-strand | 183-187 | 5 | 21 |
| β-strand | 198-201 | 4 | 21 |
| α-helix | 207-226 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 11 |
| α-helix | 6-7 | 2 | |
| β-strand | 17-19 | 3 | 11 |
| α-helix | 31-33 | 3 | |
| β-strand | 34-36 | 3 | 12 |
| β-strand | 43 | 1 | 13 |
| β-strand | 49 | 1 | 13 |
| β-strand | 54 | 1 | 14 |
| β-strand | 61-63 | 3 | 12 |
| β-strand | 65 | 1 | 15 |
| β-strand | 76-82 | 7 | 15 |
| β-strand | 91-96 | 6 | 15 |
| β-strand | 101-105 | 5 | 15 |
| β-strand | 107 | 1 | 16 |
| β-strand | 115-116 | 2 | 15 |
| β-strand | 118 | 1 | 17 |
| β-strand | 129-131 | 3 | 17 |
| α-helix | 136 | 1 | |
| β-strand | 140-142 | 3 | 17 |
| β-strand | 144-145 | 2 | 18 |
| β-strand | 152-154 | 3 | 18 |
| β-strand | 162-168 | 7 | 17 |
| β-strand | 171-175 | 5 | 17 |
| β-strand | 181-185 | 5 | 17 |
| β-strand | 189-192 | 4 | 17 |
| β-strand | 195 | 1 | 16 |
| α-helix | 198-202 | 5 | |
| β-strand | 204 | 1 | 11 |
| α-helix | 208-213 | 6 | |
| β-strand | 216 | 1 | 14 |
| α-helix | 217-221 | 5 | |
| α-helix | 222-224 | 3 | |
| β-strand | 245 | 1 | 19 |
| β-strand | 251 | 1 | 19 |
| α-helix | 264-266 | 3 | |
| β-strand | 267-269 | 3 | 17 |
42 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Large ribosomal subunit protein bL33 | 0 | protein | 55 | Escherichia coli BW25113 | P0A7N9 (AlphaFold model) |
| Large ribosomal subunit protein bL34 | 1 | protein | 46 | Escherichia coli BW25113 | P0A7P5 (AlphaFold model) |
| Large ribosomal subunit protein bL35 | 2 | protein | 65 | Escherichia coli BW25113 | P0A7Q1 (AlphaFold model) |
| Large ribosomal subunit protein bL36A | 3 | protein | 38 | Escherichia coli BW25113 | P0A7Q6 (AlphaFold model) |
| Large ribosomal subunit protein bL31A | 4 | protein | 70 | Escherichia coli BW25113 | P0A7M9 |
| N-Formylmethionine tRNA | 5 | RNA | 77 | Escherichia coli BW25113 | |
| 16S ribosomal RNA | A | RNA | 1534 | Escherichia coli BW25113 | |
| 30S ribosomal protein S2 | B | protein | 241 | Escherichia coli BW25113 | P0A7V0 |
| Small ribosomal subunit protein uS3 | C | protein | 233 | Escherichia coli BW25113 | P0A7V3 |
| Small ribosomal subunit protein uS4 | D | protein | 206 | Escherichia coli BW25113 | P0A7V8 |
| Small ribosomal subunit protein uS5 | E | protein | 167 | Escherichia coli BW25113 | P0A7W1 |
| 30S ribosomal protein S6, fully modified isoform | F | protein | 135 | Escherichia coli BW25113 | P02358 |
45 more molecules are not listed.
>8R6C_1 Large ribosomal subunit protein bL33 (chains 0) MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK
>8R6C_2 Large ribosomal subunit protein bL34 (chains 1) MKRTFQPSVLKRNRSHGFRARMATKNGRQVLARRRAKGRARLTVSK
>8R6C_3 Large ribosomal subunit protein bL35 (chains 2) MPKIKTVRGAAKRFKKTGKGGFKHKHANLRHILTKKATKRKRHLRPKAMVSKGDLGLVIA CLPYA
>8R6C_4 Large ribosomal subunit protein bL36A (chains 3) MKVRASVKKLCRNCKIVKRDGVIRVICSAEPKHKQRQG
>8R6C_5 Large ribosomal subunit protein bL31A (chains 4) MKKDIHPKYEEITASCSCGNVMKIRSTVGHDLNLDVCSKCHPFFTGKQRDVATGGRVDRF NKRFNIPGSK
>8R6C_6 N-Formylmethionine tRNA (chains 5) CGCGGGGUGGAGCAGCCUGGUAGCUCGUCGGGCUCAUAACCCGAAGGUCGUCGGUUCAAA UCCGGCCCCCGCAACCA
>8R6C_7 16S ribosomal RNA (chains A) AAAUUGAAGAGUUUGAUCAUGGCUCAGAUUGAACGCUGGCGGCAGGCCUAACACAUGCAA GUCGAACGGUAACAGGAAGAAGCUUGCUUCUUUGCUGACGAGUGGCGGACGGGUGAGUAA UGUCUGGGAAACUGCCUGAUGGAGGGGGAUAACUACUGGAAACGGUAGCUAAUACCGCAU AACGUCGCAAGACCAAAGAGGGGGACCUUCGGGCCUCUUGCCAUCGGAUGUGCCCAGAUG GGAUUAGCUAGUAGGUGGGGUAACGGCUCACCUAGGCGACGAUCCCUAGCUGGUCUGAGA GGAUGACCAGCCACACUGGAACUGAGACACGGUCCAGACUCCUACGGGAGGCAGCAGUGG GGAAUAUUGCACAAUGGGCGCAAGCCUGAUGCAGCCAUGCCGCGUGUAUGAAGAAGGCCU UCGGGUUGUAAAGUACUUUCAGCGGGGAGGAAGGGAGUAAAGUUAAUACCUUUGCUCAUU GACGUUACCCGCAGAAGAAGCACCGGCUAACUCCGUGCCAGCAGCCGCGGUAAUACGGAG GGUGCAAGCGUUAAUCGGAAUUACUGGGCGUAAAGCGCACGCAGGCGGUUUGUUAAGUCA GAUGUGAAAUCCCCGGGCUCAACCUGGGAACUGCAUCUGAUACUGGCAAGCUUGAGUCUC GUAGAGGGGGGUAGAAUUCCAGGUGUAGCGGUGAAAUGCGUAGAGAUCUGGAGGAAUACC GGUGGCGAAGGCGGCCCCCUGGACGAAGACUGACGCUCAGGUGCGAAAGCGUGGGGAGCA AACAGGAUUAGAUACCCUGGUAGUCCACGCCGUAAACGAUGUCGACUUGGAGGUUGUGCC CUUGAGGCGUGGCUUCCGGAGCUAACGCGUUAAGUCGACCGCCUGGGGAGUACGGCCGCA AGGUUAAAACUCAAAUGAAUUGACGGGGGCCCGCACAAGCGGUGGAGCAUGUGGUUUAAU UCGAUGCAACGCGAAGAACCUUACCUGGUCUUGACAUCCACGGAAGUUUUCAGAGAUGAG AAUGUGCCUUCGGGAACCGUGAGACAGGUGCUGCAUGGCUGUCGUCAGCUCGUGUUGUGA AAUGUUGGGUUAAGUCCCGCAACGAGCGCAACCCUUAUCCUUUGUUGCCAGCGGUCCGGC CGGGAACUCAAAGGAGACUGCCAGUGAUAAACUGGAGGAAGGUGGGGAUGACGUCAAGUC AUCAUGGCCCUUACGACCAGGGCUACACACGUGCUACAAUGGCGCAUACAAAGAGAAGCG ACCUCGCGAGAGCAAGCGGACCUCAUAAAGUGCGUCGUAGUCCGGAUUGGAGUCUGCAAC UCGACUCCAUGAAGUCGGAAUCGCUAGUAAUCGUGGAUCAGAAUGCCACGGUGAAUACGU UCCCGGGCCUUGUACACACCGCCCGUCACACCAUGGGAGUGGGUUGCAAAAGAAGUAGGU AGCUUAACCUUCGGGAGGGCGCUUACCACUUUGUGAUUCAUGACUGGGGUGAAGUCGUAA CAAGGUAACCGUAGGGGAACCUGCGGUUGGAUCA
>8R6C_8 30S ribosomal protein S2 (chains B) MATVSMRDMLKAGVHFGHQTRYWNPKMKPFIFGARNKVHIINLEKTVPMFNEALAELNKI ASRKGKILFVGTKRAASEAVKDAALSCDQFFVNHRWLGGMLTNWKTVRQSIKRLKDLETQ SQDGTFDKLTKKEALMRTRELEKLENSLGGIKDMGGLPDALFVIDADHEHIAIKEANNLG IPVFAIVDTNSDPDGVDFVIPGNDDAIRAVTLYLGAVAATVREGRSQDLASQAEESFVEA E
>8R6C_9 Small ribosomal subunit protein uS3 (chains C) MGQKVHPNGIRLGIVKPWNSTWFANTKEFADNLDSDFKVRQYLTKELAKASVSRIVIERP AKSIRVTIHTARPGIVIGKKGEDVEKLRKVVADIAGVPAQINIAEVRKPELDAKLVADSI TSQLERRVMFRRAMKRAVQNAMRLGAKGIKVEVSGRLGGAEIARTEWYREGRVPLHTLRA DIDYNTSEAHTTYGVIGVKVWIFKGEILGGMAAVEQPEKPAAQPKKQQRKGRK
>8R6C_10 Small ribosomal subunit protein uS4 (chains D) MARYLGPKLKLSRREGTDLFLKSGVRAIDTKCKIEQAPGQHGARKPRLSDYGVQLREKQK VRRIYGVLERQFRNYYKEAARLKGNTGENLLALLEGRLDNVVYRMGFGATRAEARQLVSH KAIMVNGRVVNIASYQVSPNDVVSIREKAKKQSRVKAALELAEQREKPTWLEVDAGKMEG TFKRKPERSDLSADINEHLIVELYSK
>8R6C_11 Small ribosomal subunit protein uS5 (chains E) MAHIEKQAGELQEKLIAVNRVSKTVKGGRIFSFTALTVVGDGNGRVGFGYGKAREVPAAI QKAMEKARRNMINVALNNGTLQHPVKGVHTGSRVFMQPASEGTGIIAGGAMRAVLEVAGV HNVLAKAYGSTNPINVVRATIDGLENMNSPEMVAAKRGKSVEEILGK
>8R6C_12 30S ribosomal protein S6, fully modified isoform (chains F) MRHYEIVFMVHPDQSEQVPGMIERYTAAITGAEGKIHRLEDWGRRQLAYPINKLHKAHYV LMNVEAPQEVIDELETTFRFNDAVIRSMVMRTKHAVTEASPMVKAKDERRERRDDFANET ADDAEAGDSEEEEEE
Water and common crystallization additives (K) are not listed.
Paenilamicins from the honey bee pathogen Paenibacillus larvae are context-specific translocation inhibitors of protein synthesis. Koller, T.O., Berger, M.J., Morici, M. et al. bioRxiv (2024). DOI 10.1101/2024.05.21.595107 · PubMed
Other PDB entries of the same protein (UniProt P0A7N9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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