ttSlyD with W4A pseudo-wild-type S2 peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Mar 2022.
Explore 7OXI in 3D Show helices and sheets RCSB PDB PDBe
7OXI contains 9 α-helices and 13 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 |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| β-strand | 7-17 | 11 | 2 |
| β-strand | 20-30 | 11 | 2 |
| β-strand | 36 | 1 | 3 |
| α-helix | 38-44 | 7 | |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 1 |
| β-strand | 52-57 | 6 | 2 |
| α-helix | 59-61 | 3 | |
| α-helix | 65-67 | 3 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 4 |
| α-helix | 76-78 | 3 | |
| β-strand | 90-94 | 5 | 4 |
| β-strand | 100-109 | 10 | 4 |
| β-strand | 112-116 | 5 | 4 |
| β-strand | 126-137 | 12 | 2 |
| α-helix | 138-139 | 2 | |
| α-helix | 140-145 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| β-strand | 9 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase | A | protein | 158 | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) | Q5SLE7 (AlphaFold model) |
| 30S ribosomal protein S2 | B, C | protein | 15 | Escherichia coli (strain K12) | P0A7V0 (AlphaFold model) |
>7OXI_1 Peptidyl-prolyl cis-trans isomerase (chains A) MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE KAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDMEGNPMPLTVVAVEGEEVTVDFNHP LAGKDLDFQVEVVKVREATPEELLHGHAHPSGHHHHHH
>7OXI_2 30S ribosomal protein S2 (chains B, C) TRYANAKMLPFAFGA
Impact of distant peptide substrate residues on enzymatic activity of SlyD. Pazicky, S., Werle, A.A., Lei, J. et al. Cell Mol Life Sci (2022) 79:138-138. DOI 10.1007/s00018-022-04179-4 · PubMed
Other PDB entries of the same protein (UniProt Q5SLE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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