Crystal structure of Mrt4. Determined by X-ray diffraction at 1.8 Å resolution. Released 26 Mar 2014.
Explore 4NWB in 3D Show helices and sheets RCSB PDB PDBe
4NWB contains 22 α-helices and 16 β-strands across 1 chain. 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 | 8-15 | 8 | |
| α-helix | 26-33 | 8 | |
| α-helix | 34-36 | 3 | |
| β-strand | 39-46 | 8 | 1 |
| α-helix | 50-59 | 10 | |
| β-strand | 64-66 | 3 | 1 |
| α-helix | 70-77 | 8 | |
| α-helix | 89-95 | 7 | |
| β-strand | 100-105 | 6 | 1 |
| α-helix | 109-118 | 10 | |
| β-strand | 121-123 | 3 | 2 |
| α-helix | 124-126 | 3 | |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 131 | 1 | |
| β-strand | 135-137 | 3 | 4 |
| α-helix | 138 | 1 | |
| β-strand | 140-141 | 2 | 5 |
| α-helix | 142 | 1 | |
| β-strand | 143 | 1 | 6 |
| α-helix | 151-153 | 3 | |
| β-strand | 156 | 1 | 6 |
| α-helix | 157-158 | 2 | |
| α-helix | 159-161 | 3 | |
| α-helix | 162-167 | 6 | |
| β-strand | 172-175 | 4 | 5 |
| β-strand | 178-181 | 4 | 5 |
| β-strand | 192-195 | 4 | 4 |
| α-helix | 199 | 1 | |
| β-strand | 200 | 1 | 3 |
| α-helix | 201 | 1 | |
| α-helix | 203-211 | 9 | |
| β-strand | 217-219 | 3 | 2 |
| β-strand | 220-228 | 9 | 1 |
| β-strand | 233-236 | 4 | 1 |
| α-helix | 237 | 1 | |
| α-helix | 238-241 | 4 | |
| α-helix | 244-248 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| mRNA turnover protein 4 | A | protein | 278 | Chaetomium thermophilum | G0S616 (AlphaFold model) |
>4NWB_1 mRNA turnover protein 4 (chains A) MPKSKRARVYHLTQVNKKGREAKERLFSNIRETIPKYQHCFVFSVDNMRNNYLKDVRHEL NDCRIFFGKTKLMARALGTTPEEEQADGLHRLTRYLTGTVGLLFTNRDPADIESYFSNLS QVDFARAGTVAPRTVTVPPGIVYSTGGEVPPEHDVPVSHTLEPELRRLGMPVRMIKGKVC LGDEKGEASEGYTICKEGEVLDSRQTRLLKLFSICLSEFKVSLLGYWSSASGEVTELEAG KTRPKREGNRRQAMNGDEMDEDQSSDEDSDGSHHHHHH
60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle. Leidig, C., Thoms, M., Holdermann, I. et al. Nat Commun (2014) 5:3491-3491. DOI 10.1038/ncomms4491 · PubMed
Other PDB entries of the same protein (UniProt G0S616 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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