Mutant ribosomal protein L1 lacking ala158 from thermus thermophilus. Determined by X-ray diffraction at 1.95 Å resolution. Released 7 Dec 2011.
Explore 3TG8 in 3D Show helices and sheets RCSB PDB PDBe
3TG8 contains 14 α-helices and 12 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 | 18-19 | 2 | |
| β-strand | 20 | 1 | 1 |
| α-helix | 21 | 1 | |
| α-helix | 22-31 | 10 | |
| α-helix | 39 | 1 | |
| β-strand | 40-47 | 8 | 2 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-63 | 5 | 3 |
| α-helix | 69-71 | 3 | |
| β-strand | 74-77 | 4 | 4 |
| α-helix | 81-88 | 8 | |
| β-strand | 93-95 | 3 | 4 |
| α-helix | 97-99 | 3 | |
| α-helix | 100-104 | 5 | |
| β-strand | 112-115 | 4 | 4 |
| α-helix | 117-119 | 3 | |
| α-helix | 120-131 | 12 | |
| α-helix | 140-142 | 3 | |
| β-strand | 145 | 1 | 4 |
| α-helix | 149-156 | 8 | |
| β-strand | 160-164 | 5 | 3 |
| β-strand | 170-177 | 8 | 2 |
| α-helix | 182-198 | 17 | |
| β-strand | 209-216 | 8 | 2 |
| β-strand | 221-223 | 3 | 2 |
| β-strand | 224 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 50S ribosomal protein L1 | A | protein | 228 | Thermus thermophilus | Q5SLP7 (AlphaFold model) |
>3TG8_1 50S ribosomal protein L1 (chains A) MPKHGKRYRALLEKVDPNKIYTIDEAAHLVKELATAKFDETVEVHAKLGIDPRRSDQNVR GTVSLPHGLGKQVRVLAIAKGEKIKEAEEAGADYVGGEEIIQKILDGWMDFDAVVATPDV MGAVGSKLGRILGPRGLLPNPKAGTVGFNIGEIIREIKGRIEFRNDKTGAIHAPVGKASF PPEKLADNIRAFIRALEAHKPEGAKGTFLRSVYVTTTMGPSVRINPHS
Structural analysis of interdomain mobility in ribosomal L1 proteins. Tishchenko, S., Nikonova, E., Kostareva, O. et al. Acta Crystallogr D Biol Crystallogr (2011) 67:1023-1027. DOI 10.1107/S0907444911043435 · PubMed
Other PDB entries of the same protein (UniProt Q5SLP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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