Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4). Determined by X-ray diffraction at 2.4 Å resolution. Released 15 Feb 2017.
Explore 5TQB in 3D Show helices and sheets RCSB PDB PDBe
5TQB contains 35 α-helices and 8 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 | 6-10 | 5 | 1 |
| β-strand | 16-22 | 7 | 1 |
| α-helix | 25-28 | 4 | |
| α-helix | 35-39 | 5 | |
| β-strand | 52-53 | 2 | 2 |
| α-helix | 54-55 | 2 | |
| α-helix | 61-63 | 3 | |
| α-helix | 75-77 | 3 | |
| α-helix | 90-97 | 8 | |
| β-strand | 105-106 | 2 | 2 |
| α-helix | 112-129 | 18 | |
| α-helix | 133-138 | 6 | |
| β-strand | 151-153 | 3 | 1 |
| α-helix | 155-157 | 3 | |
| α-helix | 166-176 | 11 | |
| α-helix | 179-185 | 7 | |
| β-strand | 210-213 | 4 | 1 |
| α-helix | 215-218 | 4 | |
| α-helix | 221-226 | 6 | |
| β-strand | 233-236 | 4 | 1 |
| α-helix | 237-239 | 3 | |
| α-helix | 242-245 | 4 | |
| α-helix | 247-249 | 3 | |
| β-strand | 255-258 | 4 | 1 |
| α-helix | 259-271 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-42 | 13 | |
| α-helix | 46-58 | 13 | |
| α-helix | 67-80 | 14 | |
| α-helix | 84-97 | 14 | |
| α-helix | 105-108 | 4 | |
| α-helix | 112-120 | 9 | |
| α-helix | 126-151 | 26 | |
| α-helix | 157-182 | 26 | |
| α-helix | 192-206 | 15 | |
| α-helix | 211-223 | 13 | |
| α-helix | 227-238 | 12 | |
| α-helix | 252-253 | 2 | |
| α-helix | 254-266 | 13 | |
| α-helix | 270-283 | 14 | |
| α-helix | 288-307 | 20 | |
| α-helix | 308-310 | 3 | |
| α-helix | 317-339 | 23 | |
| α-helix | 344-359 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 60S ribosomal protein L4-like protein | A | protein | 277 | Chaetomium thermophilum | G0SFC3 (AlphaFold model) |
| Assembly chaperone of ribosomal protein L4 (Acl4) | B | protein | 335 | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) | G0S0I4 (AlphaFold model) |
>5TQB_1 60S ribosomal protein L4-like protein (chains A) MASRPTVTVFGADGKPTGATEVLPKVFSAPIRPDIVKHVHTGMAKNKRQPYAVSEKAGHQ TSAESWGTGRAVARIPRVSGGGTHRAGQGAFGNMCRSGRMFAPTKIWRKWHVKINQGQKR FATASALAASAVAPLLMARGHQVSTVPEVPLVVDSAAVAGDAVAKTAAAYKLLKAIGAGP DVEKVKKSKKLRAGKGKMRGRRHRQRRGPLIVYSPEHDGKELVKGFRNIPGVETCPVDAL NLLQLAPGGHLGRFIVWTSAAIKQLDAVYESKKGFFL
>5TQB_2 Assembly chaperone of ribosomal protein L4 (Acl4) (chains B) SINPKELLDRATTLLEEGDIETAAKVARTAYEHIGENGRHAGAALTLLGQIHVELGDIDA ARNYYAAAVKVDEDGSLPEELGGGPEKFLWLAQLSEEGGHDSVAWFERGATVLRAQIQSL MDSLEQRPLSRGQVEAAIADKRRRLAETLCAVVEVYMTDLSWEDDAEQRCEALITEATMI APEWPETWQTVANVRISQERTEEAREALRRSLGLWTHLPPEDPGVPPFPSRVSLVRLLIE VDMEEEALEVTERLIAEDDLSVEVWYLGGYARYRLGEKEREASGQASEPEAWKDTWRSSR KWLRQCLKVFEAEEYEDERLGEHAKELIASIIGEL
Molecular basis for protection of ribosomal protein L4 from cellular degradation. Huber, F.M., Hoelz, A. Nat Commun (2017) 8:14354-14354. DOI 10.1038/ncomms14354 · PubMed
Other PDB entries of the same protein (UniProt G0SFC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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