Structure of the human SRP68-RBD. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Apr 2014.
Explore 4P3F in 3D Show helices and sheets RCSB PDB PDBe
4P3F contains 18 α-helices and 6 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 |
|---|---|---|---|
| β-strand | 50 | 1 | 1 |
| α-helix | 54-64 | 11 | |
| α-helix | 67-69 | 3 | |
| α-helix | 72-95 | 24 | |
| α-helix | 106-107 | 2 | |
| α-helix | 114-135 | 22 | |
| α-helix | 143-164 | 22 | |
| β-strand | 170 | 1 | 1 |
| α-helix | 172-192 | 21 | |
| α-helix | 196-214 | 19 | |
| α-helix | 219-243 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 50 | 1 | 2 |
| α-helix | 54-64 | 11 | |
| α-helix | 67-69 | 3 | |
| α-helix | 72-95 | 24 | |
| β-strand | 97 | 1 | 3 |
| β-strand | 104 | 1 | 3 |
| α-helix | 114-137 | 24 | |
| α-helix | 141-143 | 3 | |
| α-helix | 144-165 | 22 | |
| β-strand | 170 | 1 | 2 |
| α-helix | 172-192 | 21 | |
| α-helix | 196-215 | 20 | |
| α-helix | 219-240 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Signal recognition particle subunit SRP68 | A, B | protein | 216 | Homo sapiens | Q9UHB9 (AlphaFold model) |
>4P3F_1 Signal recognition particle subunit SRP68 (chains A, B) MGHHHHHHGSKANKEFGDSLSLEILQIIKESQQQHGLRHGDFQRYRGYCSRRQRRLRKTL NFKMGNRHKFTGKKVTEDLLTDNRYLLLVLMDAERAWSYAMQLKQEANTEPRKRFHLLSR LRKAVKHAEELERLCESNRVDAKTKLEAQAYTAYLSGMLRFEHQEWKAAIEAFNKCKTIY EKLASAFTEEQAVLYNQRVEEISPNIRYCAYNIGDQ
SRP RNA remodeling by SRP68 explains its role in protein translocation. Grotwinkel, J.T., Wild, K., Segnitz, B. et al. Science (2014) 344:101-104. DOI 10.1126/science.1249094 · 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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