Co-crystal structure of the ternary complex of human FKBP12, QDPR and Compound 4. Determined by X-ray diffraction at 1.39 Å resolution. Released 8 Oct 2025.
Explore 9DTW in 3D Show helices and sheets RCSB PDB PDBe
9DTW contains 17 α-helices and 20 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 | 12-16 | 5 | 1 |
| α-helix | 21-32 | 12 | |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 50-53 | 4 | 1 |
| α-helix | 54-56 | 3 | |
| α-helix | 60-75 | 16 | |
| β-strand | 80-85 | 6 | 1 |
| β-strand | 93 | 1 | 2 |
| α-helix | 100-107 | 8 | |
| α-helix | 108-113 | 6 | |
| α-helix | 114-125 | 12 | |
| β-strand | 126-135 | 10 | 1 |
| α-helix | 138-141 | 4 | |
| β-strand | 147 | 1 | 2 |
| α-helix | 148-165 | 18 | |
| α-helix | 171-172 | 2 | |
| β-strand | 176-182 | 7 | 1 |
| β-strand | 185-186 | 2 | 3 |
| α-helix | 188-193 | 6 | |
| α-helix | 199-201 | 3 | |
| β-strand | 203-204 | 2 | 3 |
| α-helix | 205-217 | 13 | |
| α-helix | 221-223 | 3 | |
| β-strand | 227-233 | 7 | 1 |
| β-strand | 236-242 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 4 |
| α-helix | 20 | 1 | |
| β-strand | 21-30 | 10 | 4 |
| β-strand | 35-38 | 4 | 4 |
| α-helix | 39-42 | 4 | |
| β-strand | 46-49 | 4 | 4 |
| α-helix | 57-63 | 7 | |
| β-strand | 71-76 | 6 | 4 |
| α-helix | 78-80 | 3 | |
| β-strand | 87 | 1 | 5 |
| β-strand | 91 | 1 | 5 |
| β-strand | 97-106 | 10 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dihydropteridine reductase | A | protein | 245 | Homo sapiens | P09417 (AlphaFold model) |
| Peptidyl-prolyl cis-trans isomerase FKBP1A | B | protein | 109 | Homo sapiens | P62942 (AlphaFold model) |
>9DTW_1 Dihydropteridine reductase (chains A) GMAAAAAAGEARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTDS FTEQADQVTAEVGKLLGEEKVDAILCVAGGWAGGNAKSKSLFKNCDLMWKQSIWTSTISS HLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPPGAAAIA VLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVTTEGRTEL TPAYF
>9DTW_2 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains B) SMGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRG WEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1BB9 | (2S)-N-[(2R)-1-({[(1R)-6-(4-[(4S)-5,6-dihydro[1,2,4]triazolo[1,5-a]pyrazin-7(8H… | C47 H67 N15 O5 | 1 |
Water and common crystallization additives (GOL, CL) are not listed.
Ternary complex DNA-encoded library screening uncovers FKBP molecular glues. Zandi, T.A., Tan, Z.R., Romanowski, M.J. et al. To be published.
Other PDB entries of the same protein (UniProt P09417 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9DTW 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.