FKBP12 in complex with PROTAC 6a2. Determined by X-ray diffraction at 1.2 Å resolution. Released 15 Nov 2023.
Explore 8PDF in 3D Show helices and sheets RCSB PDB PDBe
8PDF contains 5 α-helices and 8 β-strands across 1 chain. 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 | 2-8 | 7 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-30 | 10 | 1 |
| β-strand | 35-38 | 4 | 1 |
| β-strand | 46-49 | 4 | 1 |
| α-helix | 57-62 | 6 | |
| α-helix | 63-65 | 3 | |
| α-helix | 66-67 | 2 | |
| β-strand | 71-76 | 6 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 87 | 1 | 2 |
| β-strand | 91 | 1 | 2 |
| β-strand | 97-106 | 10 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase FKBP1A | A | protein | 107 | Homo sapiens | P62942 (AlphaFold model) |
>8PDF_1 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains A) GVQVETISPGDGRTFPKRGQTVVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y5Q | (2~{S},4~{R})-1-[(2~{S})-2-[2-[2-[2-[4-[(1~{S})-1-[(1~{S},5~{S},6~{R})-10-[3,5-… | C48 H61 Cl2 N9 O9 S2 | 1 |
Discovery of a Potent Proteolysis Targeting Chimera Enables Targeting the Scaffolding Functions of FK506-Binding Protein 51 (FKBP51). Geiger, T.M., Walz, M., Meyners, C. et al. Angew Chem Int Ed Engl (2024) 63:e202309706-e202309706. DOI 10.1002/anie.202309706 · PubMed
Other PDB entries of the same protein (UniProt P62942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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