The structure of a protein conducting channel. Determined by X-ray diffraction at 3.2 Å resolution. Released 6 Jan 2004.
Explore 1RH5 in 3D Show helices and sheets RCSB PDB PDBe
1RH5 contains 23 α-helices and 7 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 | |
| α-helix | 15-17 | 3 | |
| α-helix | 23-40 | 18 | |
| β-strand | 44 | 1 | 1 |
| α-helix | 45-46 | 2 | |
| α-helix | 59-63 | 5 | |
| β-strand | 69 | 1 | 1 |
| α-helix | 76-85 | 10 | |
| α-helix | 86-93 | 8 | |
| α-helix | 101-128 | 28 | |
| α-helix | 137-164 | 28 | |
| α-helix | 169-187 | 19 | |
| α-helix | 192-199 | 8 | |
| α-helix | 207-209 | 3 | |
| α-helix | 211-226 | 16 | |
| β-strand | 230-234 | 5 | 2 |
| β-strand | 246-250 | 5 | 2 |
| α-helix | 257-277 | 21 | |
| β-strand | 287 | 1 | 3 |
| β-strand | 292 | 1 | 3 |
| α-helix | 298-300 | 3 | |
| α-helix | 313-338 | 26 | |
| α-helix | 342-348 | 7 | |
| α-helix | 363-395 | 33 | |
| α-helix | 402-419 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-23 | 11 | |
| β-strand | 25-26 | 2 | 2 |
| α-helix | 27-29 | 3 | |
| α-helix | 30-65 | 36 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-49 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Preprotein translocase secY subunit | A | protein | 436 | Methanocaldococcus jannaschii | Q60175 (AlphaFold model) |
| Preprotein translocase secE subunit | B | protein | 74 | Methanocaldococcus jannaschii | Q57817 (AlphaFold model) |
| SecBeta | C | protein | 53 | Methanocaldococcus jannaschii | P60460 (AlphaFold model) |
>1RH5_1 Preprotein translocase secY subunit (chains A) MKKLIPILEKIPEVELPVKEITFKEKLKWTGIVLVLYFIMGCIDVYTAGAQIPAIFEFWQ TITASRIGTLITLGIGPIVTAGIIMQLLVGSGIIQMDLSIPENRALFQGCQKLLSIIMCF VEAVLFVGAGAFGILTPLLAFLVIIQIAFGSIILIYLDEIVSKYGIGSGIGLFIAAGVSQ TIFVGALGPEGYLWKFLNSLIQGVPNIEYIAPIIGTIIVFLMVVYAECMRVEIPLAHGRI KGAVGKYPIKFVYVSNIPVILAAALFANIQLWGLALYRMGIPILGHYEGGRAVDGIAYYL STPYGLSSVISDPIHAIVYMIAMIITCVMFGIFWVETTGLDPKSMAKRIGSLGMAIKGFR KSEKAIEHRLKRYIPPLTVMSSAFVGFLATIANFIGALGGGTGVLLTVSIVYRMYEQLLR ERTSELHPAIAKLLNK
>1RH5_2 Preprotein translocase secE subunit (chains B) MKTDFNQKIEQLKEFIEECRRVWLVLKKPTKDEYLAVAKVTALGISLLGIIGYIIHVPAT YIKGILKPPTTPRV
>1RH5_3 SecBeta (chains C) MSKREETGLATSAGLIRYMDETFSKIRVKPEHVIGVTVAFVIIEAILTYGRFL
X-ray structure of a protein-conducting channel. van den Berg, B., Clemons Jr., W.M., Collinson, I. et al. Nature (2004) 427:36-44. DOI 10.1038/nature02218 · 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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