Structure of the human SRP68-72 protein-binding domain complex. Determined by X-ray diffraction at 1.6 Å resolution. Released 7 Dec 2016.
Explore 5M72 in 3D Show helices and sheets RCSB PDB PDBe
5M72 contains 13 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 | 11-23 | 13 | |
| α-helix | 27-40 | 14 | |
| α-helix | 45-57 | 13 | |
| α-helix | 61-70 | 10 | |
| α-helix | 72-75 | 4 | |
| α-helix | 81-90 | 10 | |
| α-helix | 94-102 | 9 | |
| α-helix | 109-121 | 13 | |
| α-helix | 125-138 | 14 | |
| α-helix | 144-158 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 593-597 | 5 | |
| α-helix | 600-602 | 3 | |
| α-helix | 604-606 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle subunit SRP72 | A | protein | 160 | Homo sapiens | O76094 (AlphaFold model) |
| Signal recognition particle subunit SRP68 | B | protein | 71 | Homo sapiens | Q9UHB9 (AlphaFold model) |
>5M72_1 Signal recognition particle subunit SRP72 (chains A) GSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVI NTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDEC LAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPGS
>5M72_2 Signal recognition particle subunit SRP68 (chains B) MGSQVKDNKPLVERFETFCLDPSLVTKQANLVHFPPGFQPIPCKPLFFDLALNHVAFPPL EDKLEQKTKSG
Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction. Becker, M.M., Lapouge, K., Segnitz, B. et al. Nucleic Acids Res (2017) 45:470-481. DOI 10.1093/nar/gkw1124 · PubMed
Other PDB entries of the same protein (UniProt O76094 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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