Complex structure of human SRP72/SRP68. Determined by X-ray diffraction at 1.7 Å resolution. Released 21 Jun 2017.
Explore 5WRV in 3D Show helices and sheets RCSB PDB PDBe
5WRV contains 12 α-helices and 0 β-strands across 2 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 | 593-597 | 5 | |
| α-helix | 600-602 | 3 | |
| α-helix | 604-607 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-23 | 13 | |
| α-helix | 27-40 | 14 | |
| α-helix | 45-57 | 13 | |
| α-helix | 61-69 | 9 | |
| α-helix | 81-90 | 10 | |
| α-helix | 94-102 | 9 | |
| α-helix | 109-121 | 13 | |
| α-helix | 125-138 | 14 | |
| α-helix | 144-159 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle subunit SRP68 | A | protein | 106 | Homo sapiens | Q9UHB9 (AlphaFold model) |
| Signal recognition particle subunit SRP72 | B | protein | 163 | Homo sapiens | O76094 (AlphaFold model) |
>5WRV_1 Signal recognition particle subunit SRP68 (chains A) DLPDVQELITQVRSEKCSLQAAAILDANDAHQTETSSSQVKDNKPLVERFETFCLDPSLV TKQANLVHFPPGFQPIPCKPLFFDLALNHVAFPPLEDKLAAATKSG
>5WRV_2 Signal recognition particle subunit SRP72 (chains B) MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGS FKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLY RLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEK
Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation. Gao, Y., Zhang, Q., Lang, Y. et al. J Mol Cell Biol (2017) 9:220-230. DOI 10.1093/jmcb/mjx010 · PubMed
Other PDB entries of the same protein (UniProt Q9UHB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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