ttSlyD with pseudo-wild-type S2 peptide. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Mar 2022.
Explore 7OXH in 3D Show helices and sheets RCSB PDB PDBe
7OXH contains 7 α-helices and 13 β-strands across 2 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 | 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 | |
| β-strand | 152-153 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9 | 1 | 3 |
| 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 | protein | 15 | Escherichia coli (strain K12) | P0A7V0 (AlphaFold model) |
| Fragment of 30S ribosomal protein S2 peptide | E | protein | 2 | synthetic construct |
>7OXH_1 Peptidyl-prolyl cis-trans isomerase (chains A) MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE KAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDMEGNPMPLTVVAVEGEEVTVDFNHP LAGKDLDFQVEVVKVREATPEELLHGHAHPSGHHHHHH
>7OXH_2 30S ribosomal protein S2 (chains B) TRYWNAKMLPFAFGA
>7OXH_3 Fragment of 30S ribosomal protein S2 peptide (chains E) XX
| ID | Name | Formula | Copies |
|---|---|---|---|
| PE4 | 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha… | C16 H34 O8 | 3 |
| NI | Nickel (II) ion | Ni | 2 |
Water and common crystallization additives (PEG, CL) are not listed.
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:
MolViewer shows 7OXH directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.