Structure of SlyD from Thermus thermophilus in complex with S2 peptide. Determined by X-ray diffraction at 2.92 Å resolution. Released 14 Jan 2015.
Explore 4ODL in 3D Show helices and sheets RCSB PDB PDBe
4ODL contains 16 α-helices and 25 β-strands across 6 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 | 7-17 | 11 | 1 |
| β-strand | 20-30 | 11 | 1 |
| β-strand | 36 | 1 | 2 |
| α-helix | 38-44 | 7 | |
| α-helix | 47-48 | 2 | |
| β-strand | 52-57 | 6 | 1 |
| α-helix | 59-61 | 3 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 3 |
| α-helix | 76-78 | 3 | |
| β-strand | 90-94 | 5 | 3 |
| β-strand | 101-109 | 9 | 3 |
| β-strand | 112-116 | 5 | 3 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-137 | 12 | 1 |
| α-helix | 138-139 | 2 | |
| α-helix | 140-145 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 4 |
| β-strand | 7-17 | 11 | 5 |
| β-strand | 20-30 | 11 | 5 |
| β-strand | 36 | 1 | 6 |
| α-helix | 38-44 | 7 | |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 4 |
| β-strand | 52-57 | 6 | 5 |
| α-helix | 59-61 | 3 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 7 |
| α-helix | 76-78 | 3 | |
| α-helix | 80 | 1 | |
| β-strand | 90-94 | 5 | 7 |
| β-strand | 100-109 | 10 | 7 |
| β-strand | 112-116 | 5 | 7 |
| β-strand | 126-137 | 12 | 5 |
| α-helix | 138-139 | 2 | |
| α-helix | 140-145 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27 | 1 | 7 |
| β-strand | 31 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-32 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase SlyD | A, B | protein | 158 | Thermus thermophilus | Q5SLE7 (AlphaFold model) |
| 30S ribosomal protein S2 | C, D, E, F | protein | 16 | Escherichia coli | P0A7V0 (AlphaFold model) |
>4ODL_1 Peptidyl-prolyl cis-trans isomerase SlyD (chains A, B) MKVGQDKVVTIRYTLQVEGEVLDQGELSYLHGHRNLIPGLEEALEGREEGEAFQAHVPAE KAYGPHDPEGVQVVPLSAFPEDAEVVPGAQFYAQDMEGNPMPLTVVAVEGEEVTVDFNHP LAGKDLDFQVEVVKVREATPEELLHGHAHPSGHHHHHH
>4ODL_2 30S ribosomal protein S2 (chains C, D, E, F) TRYWNPKMKPFIFGAX
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD. Quistgaard, E.M., Weininger, U., Ural-Blimke, Y. et al. BMC Biol (2016) 14:82-82. DOI 10.1186/s12915-016-0300-3 · 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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