2J37: Model of mammalian srp
Model of mammalian srp bound to 80S rncs. Determined by electron microscopy at 8.7 Å resolution. Released 8 Nov 2006.
- Method
- Electron microscopy
- Resolution
- 8.7 Å
- Organisms
- TRITICUM SP., TRITICUM SP, CANIS SP.
- Chains
- 8
- Atoms
- 15,110
- Mol. weight
- 248 kDa
- Released
- 8 Nov 2006
Explore 2J37 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2J37 contains 41 α-helices and 23 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 4: 3 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 76 | 1 | 1 |
| α-helix | 80-88 | 9 | |
| β-strand | 91-94 | 4 | 1 |
| α-helix | 103-113 | 11 | |
| β-strand | 117-123 | 7 | 1 |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 143-147 | 5 | |
Chain 5: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-13 | 6 | |
| α-helix | 16-38 | 23 | |
| α-helix | 46-65 | 20 | |
Chain 6: 4 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 2 |
| α-helix | 25-30 | 6 | |
| α-helix | 33-35 | 3 | |
| α-helix | 36-50 | 15 | |
| β-strand | 58-59 | 2 | 2 |
| α-helix | 61-67 | 7 | |
| β-strand | 79-86 | 8 | 2 |
| β-strand | 91-95 | 5 | 2 |
Chain B: 6 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 16-18 | 3 | 3 |
| α-helix | 20-23 | 4 | |
| β-strand | 24 | 1 | 4 |
| β-strand | 41 | 1 | 4 |
| α-helix | 46-53 | 8 | |
| α-helix | 54-56 | 3 | |
| β-strand | 59-63 | 5 | 3 |
| β-strand | 81-85 | 5 | 3 |
| β-strand | 87 | 1 | 5 |
| β-strand | 93 | 1 | 5 |
| 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 | |
Chain W: 24 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-39 | 15 | |
| α-helix | 50-60 | 11 | |
| α-helix | 71-87 | 17 | |
| β-strand | 102-107 | 6 | 6 |
| α-helix | 114-127 | 14 | |
| β-strand | 132-137 | 6 | 6 |
| α-helix | 143-155 | 13 | |
| β-strand | 159-161 | 3 | 6 |
| α-helix | 168-181 | 14 | |
| β-strand | 186-191 | 6 | 6 |
| α-helix | 192-193 | 2 | |
| α-helix | 199-212 | 14 | |
| β-strand | 216-222 | 7 | 6 |
| α-helix | 229-240 | 12 | |
| β-strand | 245-248 | 4 | 6 |
| α-helix | 258-266 | 9 | |
| β-strand | 270-274 | 5 | 6 |
| β-strand | 282-283 | 2 | 6 |
| α-helix | 287-292 | 6 | |
| α-helix | 304-307 | 4 | |
| α-helix | 326-329 | 4 | |
| α-helix | 333-338 | 6 | |
| α-helix | 358-360 | 3 | |
| α-helix | 368-379 | 12 | |
| α-helix | 384-388 | 5 | |
| α-helix | 392-398 | 7 | |
| α-helix | 401-409 | 9 | |
| α-helix | 414-428 | 15 | |
| α-helix | 439-442 | 4 | |
| α-helix | 450-458 | 9 | |
| α-helix | 466-475 | 10 | |
| α-helix | 482-487 | 6 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 60S ribosomal protein L23 | 4 | protein | 152 | TRITICUM SP. | O81229 (AlphaFold model) |
| Ribosomal protein L35 | 5 | protein | 124 | TRITICUM SP. | Q8L805 (AlphaFold model) |
| Ribosomal protein L31 | 6 | protein | 123 | TRITICUM SP | Q5XLD9 (AlphaFold model) |
| Srp RNA | A | RNA | 128 | CANIS SP. | |
| Signal recognition particle 19 kda protein (SRP19) | B | protein | 108 | HOMO SAPIENS | P09132 (AlphaFold model) |
| Signal sequence | S | protein | 17 | CANIS SP. | Q1WHN3 |
| Signal recognition particle 54 kda protein (SRP54) | W | protein | 504 | CANIS SP. | P61010 |
| Ribosomal RNA | Z | RNA | 280 | HALOARCULA MARISMORTUI | |
Sequence of entity 1 (4), FASTA
>2J37_1 60S RIBOSOMAL PROTEIN L23 (chains 4)
MAPKVAVAKKGDAKAQAAKVAKAVKSGSIKKTAKKIRTSVTFHRPKTLSKARDPKYPRIS
TPGRNKLDQYQILKYPLTTESAMKKIEDNNTLVFIVDLKADKKKIKAAVKKMYDIQAKKV
NTLIRPDGKKKAYVKLTPDYDALDVANKIGII
Sequence of entity 2 (5), FASTA
>2J37_2 RIBOSOMAL PROTEIN L35 (chains 5)
MSSGKVKAGELWNKSKDDLTKQLAELKTELGQLRIQKVASSGSKLNRIHDIRKSIARVLT
VINAKQRAQLRLFYKNKKYAPLDLRAKQTRAIRRRLSPDEKSRVLEKTKKRTVHFPQRKF
AIKA
Sequence of entity 3 (6), FASTA
>2J37_3 RIBOSOMAL PROTEIN L31 (chains 6)
MSEKKRAPGPRKDEVVTREYTVNLHKRLHGCTFKKKAPNAIKEIRKFAQKAMGTNDVRID
VKLNKHIWSSGIRSVPRRVRVRIARKRNDEEDAKEELYSLVTVAEVPQEGLKGLGTKVVE
DED
Sequence of entity 4 (A), FASTA
>2J37_4 SRP RNA (chains A)
GACACUAAGUUCGGCAUCAAUAUGGUGACCUCCCGGGAGCGGGGGACCACCAGGUUGCCU
AAGGAGGGGUGAACCGGCCCAGGUCGGAAACGGAGCAGGUCAAAACUCCCGUGCUGAUCA
GUAGUGUC
Sequence of entity 5 (B), FASTA
>2J37_5 SIGNAL RECOGNITION PARTICLE 19 KDA PROTEIN (SRP19) (chains B)
MRFICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNKMYSREW
NRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQ
Sequence of entity 6 (S), FASTA
>2J37_6 SIGNAL SEQUENCE (chains S)
LGFPINFLTLYVTVQHK
Sequence of entity 7 (W), FASTA
>2J37_7 SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN (SRP54) (chains W)
MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAI
DLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSK
LAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFK
NENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKV
DVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDI
EGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFM
SKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQEL
LTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGL
QSMMRQFQQGAAGNMKGMMGFNNM
Sequence of entity 8 (Z), FASTA
>2J37_8 RIBOSOMAL RNA (chains Z)
CUGCAAAGUACCCUCAGAAGGGAGGCGAAAUAGAGCACAGCGAUAGUCGGGUGAGAACCC
CGACGGCCUAAUGGAUAAGGGUUCCUCAGCACUGCUGAUCAGCUGAGGGUUAGCCGGUCC
UAAGUCAUACCGCAACUCGACUAUGACGAAAUGGGAAACGGGUUAAUAUUCCCGUGCCAC
GGGGUCGAUCACGCUGGGCAUCGCCCAGUCGAACCGUCCAACUCCGUGGAAGCCGUAAUG
GCAGGAAGCGGACGAACGGCGGCAUAGGGAAACGUGAUUC
Primary citation
Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Halic, M., Blau, M., Becker, T. et al. Nature (2006) 444:507-511. DOI 10.1038/nature05326 · PubMed
Other PDB entries of the same protein (UniProt O81229 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2GO5 7.4 Å, Structure of signal recognition particle receptor (SR) in complex with signal…
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