p110delta/p85alpha with taselisib (GDC-0032). Determined by X-ray diffraction at 2.91 Å resolution. Released 11 Jan 2017.
Explore 5T8F in 3D Show helices and sheets RCSB PDB PDBe
5T8F contains 56 α-helices and 48 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 | 19-25 | 7 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 41 | 1 | 2 |
| α-helix | 42-53 | 12 | |
| α-helix | 59-61 | 3 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 74 | 1 | 3 |
| β-strand | 79-81 | 3 | 1 |
| β-strand | 88 | 1 | 2 |
| α-helix | 89-92 | 4 | |
| β-strand | 94 | 1 | 3 |
| β-strand | 98-103 | 6 | 1 |
| α-helix | 108-121 | 14 | |
| α-helix | 126-130 | 5 | |
| α-helix | 134-156 | 23 | |
| α-helix | 159-166 | 8 | |
| β-strand | 171 | 1 | 4 |
| β-strand | 189 | 1 | 5 |
| β-strand | 192-196 | 5 | 6 |
| β-strand | 202-205 | 4 | 6 |
| β-strand | 208 | 1 | 5 |
| α-helix | 213-221 | 9 | |
| α-helix | 236-238 | 3 | |
| β-strand | 239-243 | 5 | 6 |
| β-strand | 246 | 1 | 7 |
| β-strand | 249-250 | 2 | 6 |
| α-helix | 256-258 | 3 | |
| β-strand | 259 | 1 | 4 |
| α-helix | 260-268 | 9 | |
| α-helix | 270-272 | 3 | |
| β-strand | 273-278 | 6 | 6 |
| α-helix | 279-286 | 8 | |
| β-strand | 322-331 | 10 | 8 |
| β-strand | 340-349 | 10 | 9 |
| β-strand | 352-353 | 2 | 9 |
| α-helix | 356-358 | 3 | |
| β-strand | 359 | 1 | 9 |
| β-strand | 363-364 | 2 | 9 |
| α-helix | 365 | 1 | |
| β-strand | 370-380 | 11 | 8 |
| β-strand | 389-397 | 9 | 9 |
| β-strand | 416-424 | 9 | 9 |
| β-strand | 426 | 1 | 10 |
| β-strand | 431 | 1 | 11 |
| β-strand | 432 | 1 | 10 |
| α-helix | 433 | 1 | |
| β-strand | 435-440 | 6 | 8 |
| α-helix | 441 | 1 | |
| β-strand | 442-443 | 2 | 9 |
| α-helix | 444 | 1 | |
| α-helix | 461-462 | 2 | |
| β-strand | 470-475 | 6 | 8 |
| β-strand | 484 | 1 | 11 |
| α-helix | 485-487 | 3 | |
| α-helix | 488-495 | 8 | |
| α-helix | 506-516 | 11 | |
| α-helix | 525-533 | 9 | |
| α-helix | 535-541 | 7 | |
| α-helix | 543-545 | 3 | |
| α-helix | 546-552 | 7 | |
| α-helix | 558-568 | 11 | |
| α-helix | 571-575 | 5 | |
| α-helix | 576-582 | 7 | |
| α-helix | 590-599 | 10 | |
| α-helix | 600-602 | 3 | |
| α-helix | 605-610 | 6 | |
| α-helix | 612-618 | 7 | |
| α-helix | 619-621 | 3 | |
| α-helix | 628-639 | 12 | |
| α-helix | 641-652 | 12 | |
| α-helix | 658-674 | 17 | |
| α-helix | 676-705 | 30 | |
| α-helix | 708-720 | 13 | |
| α-helix | 722-728 | 7 | |
| β-strand | 731-733 | 3 | 12 |
| β-strand | 736-741 | 6 | 12 |
| β-strand | 743-744 | 2 | 13 |
| β-strand | 750-751 | 2 | 14 |
| β-strand | 759-762 | 4 | 14 |
| β-strand | 763-764 | 2 | 13 |
| β-strand | 775-780 | 6 | 14 |
| α-helix | 785-802 | 18 | |
| β-strand | 815-819 | 5 | 14 |
| β-strand | 822-826 | 5 | 14 |
| β-strand | 831-833 | 3 | 15 |
| α-helix | 834-839 | 6 | |
| α-helix | 855-862 | 8 | |
| α-helix | 867-889 | 23 | |
| α-helix | 896-898 | 3 | |
| β-strand | 899-902 | 4 | 15 |
| β-strand | 907-909 | 3 | 15 |
| α-helix | 929-932 | 4 | |
| α-helix | 936-942 | 7 | |
| α-helix | 950-969 | 20 | |
| α-helix | 971-981 | 11 | |
| α-helix | 982-984 | 3 | |
| β-strand | 986 | 1 | 16 |
| β-strand | 989 | 1 | 16 |
| α-helix | 992-1001 | 10 | |
| α-helix | 1008-1030 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 442-513 | 72 | |
| α-helix | 518-587 | 70 | |
| α-helix | 591-598 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform | A | protein | 1015 | Homo sapiens | O00329 (AlphaFold model) |
| Phosphatidylinositol 3-kinase regulatory subunit alpha | B | protein | 169 | Bos taurus | P23727 (AlphaFold model) |
>5T8F_1 Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (chains A) NQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQT AEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEV NDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKF EGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPL CQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSL WSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLE FDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGE RCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGR HSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWN KHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLV QVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGST HHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLD PSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQL MDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALL NWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFL GNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLH LFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKV
>5T8F_2 Phosphatidylinositol 3-kinase regulatory subunit alpha (chains B) YQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEDYTRTSQEIQMKRTAIEAFNET IKIFEEQCQTQERYSKEYIEKFKREGNETEIQRIMHNYEKLKSRISEIVDSRRRLEEDLK KQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 799 | 2-methyl-2-(4-{2-[3-methyl-1-(propan-2-yl)-1H-1,2,4-triazol-5-yl]-5,6-dihydroim… | C24 H28 N8 O2 | 1 |
Structure-Based Design of Tricyclic NF-kappa B Inducing Kinase (NIK) Inhibitors That Have High Selectivity over Phosphoinositide-3-kinase (PI3K). Castanedo, G.M., Blaquiere, N., Beresini, M. et al. J Med Chem (2017) 60:627-640. DOI 10.1021/acs.jmedchem.6b01363 · PubMed
Other PDB entries of the same protein (UniProt O00329 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5T8F 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.