Ribosomal protein L11 from Thermotoga maritima. Determined by solution NMR. Released 17 Jun 2008.
Explore 2K3F in 3D Show helices and sheets RCSB PDB PDBe
2K3F contains 9 α-helices and 5 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 |
|---|---|---|---|
| β-strand | 5-15 | 11 | 1 |
| α-helix | 24 | 1 | |
| α-helix | 25-29 | 5 | |
| α-helix | 30 | 1 | |
| α-helix | 35-45 | 11 | |
| β-strand | 52-61 | 10 | 1 |
| β-strand | 66-70 | 5 | 1 |
| α-helix | 76-79 | 4 | |
| α-helix | 80-84 | 5 | |
| β-strand | 98-100 | 3 | 2 |
| α-helix | 102-111 | 10 | |
| α-helix | 113-116 | 4 | |
| α-helix | 121-134 | 14 | |
| β-strand | 137-139 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 50S ribosomal protein L11 | A | protein | 141 | Thermotoga maritima | P29395 (AlphaFold model) |
>2K3F_1 50S ribosomal protein L11 (chains A) MAKKVAAQIKLQLPAGKATPAPPVGPALGQHGVNIMEFCKRFNAETADKAGMILPVVITV YEDKSFTFIIKTPPASFLLKKAAGIEKGSSEPKRKIVGKVTRKQIEEIAKTKMPDLNANS LEAAMKIIEGTAKSMGIEVVD
Domain reorientation and induced fit upon RNA binding: solution structure and dynamics of ribosomal protein L11 from Thermotoga maritima. Ilin, S., Hoskins, A., Ohlenschlager, O. et al. Chembiochem (2005) 6:1611-1618. DOI 10.1002/cbic.200500091 · PubMed
Other PDB entries of the same protein (UniProt P29395 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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