Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Determined by electron microscopy at 12.0 Å resolution. Released 20 Apr 2004.
Explore 1RY1 in 3D Show helices and sheets RCSB PDB PDBe
1RY1 contains 35 α-helices and 28 β-strands across 6 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 |
|---|---|---|---|
| β-strand | 16-18 | 3 | 4 |
| α-helix | 20-23 | 4 | |
| β-strand | 24 | 1 | 5 |
| β-strand | 41 | 1 | 5 |
| α-helix | 46-53 | 8 | |
| α-helix | 54-56 | 3 | |
| β-strand | 59-63 | 5 | 4 |
| β-strand | 81-85 | 5 | 4 |
| β-strand | 87 | 1 | 6 |
| β-strand | 93 | 1 | 6 |
| α-helix | 102-111 | 10 | |
| α-helix | 112-114 | 3 | |
| α-helix | 116-119 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-20 | 15 | |
| β-strand | 26-29 | 4 | 1 |
| β-strand | 31 | 1 | 2 |
| β-strand | 32 | 1 | 3 |
| β-strand | 37 | 1 | 3 |
| β-strand | 38-43 | 6 | 1 |
| β-strand | 49-53 | 5 | 1 |
| α-helix | 56-58 | 3 | |
| α-helix | 59-74 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| α-helix | 6-18 | 13 | |
| β-strand | 26 | 1 | 2 |
| β-strand | 27-33 | 7 | 1 |
| β-strand | 55-61 | 7 | 1 |
| β-strand | 66-72 | 7 | 1 |
| α-helix | 76-90 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 51-64 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 | |
| α-helix | 17-19 | 3 | |
| α-helix | 24-40 | 17 | |
| α-helix | 45-61 | 17 | |
| α-helix | 64-66 | 3 | |
| α-helix | 70-85 | 16 | |
| β-strand | 90 | 1 | 7 |
| β-strand | 99-104 | 6 | 8 |
| α-helix | 111-123 | 13 | |
| β-strand | 129-133 | 5 | 8 |
| α-helix | 139-152 | 14 | |
| β-strand | 156-158 | 3 | 8 |
| α-helix | 159-160 | 2 | |
| α-helix | 165-179 | 15 | |
| β-strand | 183-187 | 5 | 8 |
| α-helix | 188-190 | 3 | |
| α-helix | 196-209 | 14 | |
| β-strand | 213-219 | 7 | 8 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-236 | 12 | |
| β-strand | 241-245 | 5 | 8 |
| α-helix | 254-263 | 10 | |
| β-strand | 267-271 | 5 | 8 |
| β-strand | 279-281 | 3 | 8 |
| α-helix | 284-292 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 329-341 | 13 | |
| α-helix | 346-349 | 4 | |
| β-strand | 351 | 1 | 7 |
| α-helix | 366-379 | 14 | |
| α-helix | 384-388 | 5 | |
| α-helix | 392-398 | 7 | |
| α-helix | 401-409 | 9 | |
| α-helix | 414-432 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SRP Alu domain | E | RNA | 50 | Canis lupus familiaris | |
| SRP S domain | A | RNA | 128 | Canis lupus familiaris | |
| Srp RNA | M | RNA | 27 | Canis lupus familiaris | |
| Srp RNA | N | RNA | 31 | Canis lupus familiaris | |
| Srp RNA | O | RNA | 24 | Canis lupus familiaris | |
| Srp RNA | P | RNA | 20 | Canis lupus familiaris | |
| Srp RNA | Q | RNA | 12 | Canis lupus familiaris | |
| Srp RNA | R | RNA | 12 | Canis lupus familiaris | |
| SRP9 | C | protein | 85 | Canis lupus familiaris | P49458 (AlphaFold model) |
| SRP14 | D | protein | 106 | Canis lupus familiaris | P37108 (AlphaFold model) |
| SRP19 | B | protein | 108 | Canis lupus familiaris | P09132 (AlphaFold model) |
| SRP54NG | U | protein | 296 | Canis lupus familiaris | O07347 (AlphaFold model) |
2 more molecules are not listed.
>1RY1_1 SRP Alu domain (chains E) GGGCCGGGCGCGGUGGCGCGCGCCUGUAGUCCCAGCUACUCGGGAGGCUC
>1RY1_2 SRP S domain (chains A) GACACUAAGUUCGGCAUCAAUAUGGUGACCUCCCGGGAGCGGGGGACCACCAGGUUGCCU AAGGAGGGGUGAACCGGCCCAGGUCGGAAACGGAGCAGGUCAAAACUCCCGUGCUGAUCA GUAGUGUC
>1RY1_3 SRP RNA (chains M) AGGCUGGAGGAUCGCUUGAGUCCAGGA
>1RY1_4 SRP RNA (chains N) CCUGUGCAACAUAGCGAGACCCCGUCUCUUU
>1RY1_5 SRP RNA (chains O) GUUCUGGGCUGUAGUGCGCUAUGC
>1RY1_6 SRP RNA (chains P) CAAUAGCCACUGCACUCCAG
>1RY1_7 SRP RNA (chains Q) CGAUCGGGUGUC
>1RY1_8 SRP RNA (chains R) AUCGCGCCUGUG
>1RY1_9 SRP9 (chains C) PQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGNLCVKVTDDLVCLVYKTDQAQDVKK IEKFHSQLMRLMVAKEARNVTMETE
>1RY1_10 SRP14 (chains D) VLLESEQFLTELTRLFQKCRTSGSVYITLKKYDGRTKPIPKKGTVEGFEPADNKCLLRAT DGKKKISTVVSSKEVNKFQMAYSNLLRANMDGLKKRDKKNKTKKTK
>1RY1_11 SRP19 (chains B) MRFICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNKMYSREW NRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQ
>1RY1_12 SRP54NG (chains U) MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVARDFVERVREEAL GKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLAL YYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEA RDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVT GLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMGD
Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Halic, M., Becker, T., Pool, M.R. et al. Nature (2004) 427:808-814. DOI 10.1038/nature02342 · PubMed
Other PDB entries of the same protein (UniProt P49458 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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