The plug domain of the SecY protein stablizes the closed state of the translocation channel and maintains a membrane seal. Determined by X-ray diffraction at 3.5 Å resolution. Released 14 Aug 2007.
Explore 2YXQ in 3D Show helices and sheets RCSB PDB PDBe
2YXQ contains 21 α-helices and 11 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 5-10 | 6 | |
| β-strand | 14 | 1 | 1 |
| α-helix | 23-42 | 20 | |
| β-strand | 44 | 1 | 2 |
| α-helix | 45 | 1 | |
| α-helix | 54-57 | 4 | |
| β-strand | 69 | 1 | 2 |
| α-helix | 76-88 | 13 | |
| α-helix | 101-128 | 28 | |
| α-helix | 137-164 | 28 | |
| α-helix | 169-187 | 19 | |
| α-helix | 192-202 | 11 | |
| α-helix | 207-228 | 22 | |
| β-strand | 231-232 | 2 | 3 |
| β-strand | 235 | 1 | 4 |
| β-strand | 236 | 1 | 5 |
| β-strand | 243 | 1 | 5 |
| β-strand | 248-249 | 2 | 3 |
| α-helix | 253-255 | 3 | |
| α-helix | 256-275 | 20 | |
| α-helix | 295-299 | 5 | |
| α-helix | 313-335 | 23 | |
| α-helix | 342-351 | 10 | |
| β-strand | 356 | 1 | 4 |
| α-helix | 363-395 | 33 | |
| α-helix | 401-424 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-21 | 19 | |
| β-strand | 25 | 1 | 3 |
| α-helix | 27-29 | 3 | |
| α-helix | 30-64 | 35 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28 | 1 | 1 |
| α-helix | 31-47 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Preprotein translocase subunit secY | A | protein | 431 | Methanocaldococcus jannaschii | Q60175 (AlphaFold model) |
| Preprotein translocase subunit secE | B | protein | 74 | Methanocaldococcus jannaschii | Q57817 (AlphaFold model) |
| Preprotein translocase secG subunit | C | protein | 53 | Methanocaldococcus jannaschii | P60460 (AlphaFold model) |
>2YXQ_1 Preprotein translocase subunit secY (chains A) MKKLIPILEKIPEVELPVKEITFKEKLKWTGIVLVLYFIMGCIDVYTAGAQIPAIFEFWG RIGTLITLGIGPIVTAGIIMQLLVGSGIIQMDLSIPENRALFQGCQKLLSIIMCFVEAVL FVGAGAFGILTPLLAFLVIIQIAFGSIILIYLDEIVSKYGIGSGIGLFIAAGVSQTIFVG ALGPEGYLWKFLNSLIQGVPNIEYIAPIIGTIIVFLMVVYAECMRVEIPLAHGRIKGAVG KYPIKFVYVSNIPVILAAALFANIQLWGLALYRMGIPILGHYEGGRAVDGIAYYLSTPYG LSSVISDPIHAIVYMIAMIITCVMFGIFWVETTGLDPKSMAKRIGSLGMAIKGFRKSEKA IEHRLKRYIPPLTVMSSAFVGFLATIANFIGALGGGTGVLLTVSIVYRMYEQLLREKVSE LHPAIAKLLNK
>2YXQ_2 Preprotein translocase subunit secE (chains B) MKTDFNQKIEQLKEFIEECRRVWLVLKKPTKDEYLAVAKVTALGISLLGIIGYIIHVPAT YIKGILKPPTTPRV
>2YXQ_3 Preprotein translocase secG subunit (chains C) MSKREETGLATSAGLIRYMDETFSKIRVKPEHVIGVTVAFVIIEAILTYGRFL
The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal. Li, W., Schulman, S., Boyd, D. et al. Mol Cell (2007) 26:511-521. DOI 10.1016/j.molcel.2007.05.002 · PubMed
Other PDB entries of the same protein (UniProt Q60175 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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