4UE5: SRP14
Structural basis for targeting and elongation arrest of Bacillus signal recognition particle. Determined by electron microscopy at 9.0 Å resolution. Released 9 Sept 2015.
- Method
- Electron microscopy
- Resolution
- 9.0 Å
- Organism
- CANIS LUPUS FAMILIARIS
- Chains
- 7
- Atoms
- 9,948
- Mol. weight
- 199.91 kDa
- Released
- 9 Sept 2015
Explore 4UE5 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4UE5 contains 42 α-helices and 26 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.
Chain B: 2 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-19 | 14 | |
| β-strand | 21-33 | 13 | 1 |
| β-strand | 55-61 | 7 | 1 |
| β-strand | 66-72 | 7 | 1 |
| α-helix | 76-90 | 15 | |
Chain C: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-64 | 11 | |
| α-helix | 72-90 | 19 | |
| α-helix | 114-136 | 23 | |
| α-helix | 141-164 | 24 | |
| α-helix | 172-192 | 21 | |
| α-helix | 196-215 | 20 | |
| α-helix | 219-240 | 22 | |
Chain D: 24 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-18 | 16 | |
| α-helix | 25-41 | 17 | |
| α-helix | 46-57 | 12 | |
| α-helix | 58-62 | 5 | |
| α-helix | 71-86 | 16 | |
| α-helix | 93-96 | 4 | |
| β-strand | 103-108 | 6 | 2 |
| β-strand | 109 | 1 | 3 |
| β-strand | 110 | 1 | 4 |
| β-strand | 112 | 1 | 4 |
| α-helix | 114-128 | 15 | |
| β-strand | 132-136 | 5 | 2 |
| α-helix | 142-154 | 13 | |
| β-strand | 159-160 | 2 | 2 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-190 | 5 | 2 |
| β-strand | 194 | 1 | 3 |
| α-helix | 201-209 | 9 | |
| β-strand | 216-222 | 7 | 2 |
| α-helix | 223-225 | 3 | |
| α-helix | 228-239 | 12 | |
| β-strand | 243-248 | 6 | 2 |
| α-helix | 256-266 | 11 | |
| β-strand | 270-274 | 5 | 2 |
| β-strand | 282-283 | 2 | 2 |
| α-helix | 287-295 | 9 | |
| α-helix | 301-307 | 7 | |
| α-helix | 317-324 | 8 | |
| α-helix | 329-338 | 10 | |
| α-helix | 346-349 | 4 | |
| α-helix | 365-368 | 4 | |
| α-helix | 376-381 | 6 | |
| α-helix | 384-388 | 5 | |
| α-helix | 392-398 | 7 | |
| α-helix | 401-410 | 10 | |
| α-helix | 414-432 | 19 | |
Chain E: 2 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-4 | 2 | 1 |
| α-helix | 7-19 | 13 | |
| β-strand | 26-35 | 10 | 1 |
| β-strand | 37-43 | 7 | 1 |
| β-strand | 48-53 | 6 | 1 |
| α-helix | 57-72 | 16 | |
Chain F: 6 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 16-18 | 3 | 5 |
| α-helix | 20-23 | 4 | |
| β-strand | 24 | 1 | 6 |
| β-strand | 41 | 1 | 6 |
| α-helix | 46-53 | 8 | |
| α-helix | 54-56 | 3 | |
| β-strand | 59-63 | 5 | 5 |
| β-strand | 81-85 | 5 | 5 |
| β-strand | 87 | 1 | 7 |
| β-strand | 93 | 1 | 7 |
| α-helix | 102-111 | 10 | |
| α-helix | 112-114 | 3 | |
| α-helix | 116-119 | 4 | |
Chain S: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 51-64 | 14 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 7S RNA | A | RNA | 299 | CANIS LUPUS FAMILIARIS | |
| SRP14 | B | protein | 75 | CANIS LUPUS FAMILIARIS | P16255 (AlphaFold model) |
| Signal recognition particle subunit SRP68 | C | protein | 195 | CANIS LUPUS FAMILIARIS | Q00004 (AlphaFold model) |
| Signal recognition particle 54 kda protein | D | protein | 433 | CANIS LUPUS FAMILIARIS | P61010 (AlphaFold model) |
| SRP9 | E | protein | 74 | CANIS LUPUS FAMILIARIS | P21262 (AlphaFold model) |
| Signal recognition particle 9 kda protein | F | protein | 107 | CANIS LUPUS FAMILIARIS | J9PAS6 |
| Signal sequence | S | protein | 18 | CANIS LUPUS FAMILIARIS | P32308 |
Sequence of entity 1 (A), FASTA
>4UE5_1 7S RNA (chains A)
GCCGGGCGCGGUGGCGCGCGCCUGUAGUCCCAGCUACUCGGGAGGCUGAGGCAGGAGGAU
CGCUUGAGCCCAGGAGUUCUGGGCUGCAGUGCGCUAUGCCGAUCGGGUGUCCGCACUAAG
UUCGGCAUCAAUAUGGUGACCUCCCGGGAGCGGGGGACCACCAGGUUGCCUAAGGAGGGG
UGAACCGGCCCAGGUCGGAAACGGAGCAGGUCAAAACUCCCGUGCUGAUCAGUAGUGGGA
UCGCGCCUGUGAAUAGCCACUGCACUCCAGCCUGUGCAACAUAGCGAGACCCCGUCUCU
Sequence of entity 2 (B), FASTA
>4UE5_2 SRP14 (chains B)
VLLESEQFLTELTRLFQKCRLSGSVFITLKKYDNKCLLRATDGKKKISTVVSSKEVNKFQ
MAYSNLLRANMDGLK
Sequence of entity 3 (C), FASTA
>4UE5_3 SIGNAL RECOGNITION PARTICLE SUBUNIT SRP68 (chains C)
LSLEILQIIKESQQQHGLRHGDFQRYRGYCSRRQRRLRKTLNFKMGNRHKFTGKKVTEDL
LTDNRYLLLVLMDAERAWSYAMQLKQEANTEPRKRFHLLSRLRKAVKHAEELERLCESNR
VDAKTKLEAQAYTAYLSGMLRFEHQEWKAAIEAFNKCKTIYEKLASAFTEEQAVLYNQRV
EEISPNIRYCAYNIG
Sequence of entity 4 (D), FASTA
>4UE5_4 SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN (chains D)
MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAI
DLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSK
LAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFK
NENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKV
DVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDI
EGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFM
SKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQEL
LTQYTKFAQMVKK
Sequence of entity 5 (E), FASTA
>4UE5_5 SRP9 (chains E)
AQYQTWEEFSRAAEKLYLADPMKARVVLKYRHSDGSLCIKVTDDLVCLVYRTDQAQDVKK
IEKFHSQLMRLMVA
Sequence of entity 6 (F), FASTA
>4UE5_6 SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN (chains F)
RFICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNKMYSREWN
RDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQ
Sequence of entity 7 (S), FASTA
>4UE5_7 SIGNAL SEQUENCE (chains S)
LGFPINFLTLYVTVQHKK
Primary citation
Translational Arrest by a Prokaryotic Signal Recognition Particle is Mediated by RNA Interactions. Beckert, B., Kedrov, A., Sohmen, D. et al. Nat Struct Mol Biol (2015) 22:767. DOI 10.1038/NSMB.3086 · PubMed
Other PDB entries of the same protein (UniProt P16255 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7OBR 2.8 Å, RNC-SRP early complex
- 6FRK 3.7 Å, Structure of a prehandover mammalian ribosomal SRP and SRP receptor targeting complex
- 6R6G 3.7 Å, Structure of XBP1u-paused ribosome nascent chain complex with SRP.
Browse structure collections
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