Human PI3KDELTA in complex with compound 29. Determined by X-ray diffraction at 2.77 Å resolution. Released 11 Dec 2019.
Explore 6OCU in 3D Show helices and sheets RCSB PDB PDBe
6OCU contains 51 α-helices and 45 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 | 79-82 | 4 | 1 |
| β-strand | 88 | 1 | 2 |
| α-helix | 89-92 | 4 | |
| 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 | 3 |
| β-strand | 189-194 | 6 | 4 |
| β-strand | 196 | 1 | 5 |
| β-strand | 203-208 | 6 | 4 |
| α-helix | 213-220 | 8 | |
| β-strand | 239-243 | 5 | 5 |
| β-strand | 249-250 | 2 | 5 |
| α-helix | 256-258 | 3 | |
| β-strand | 259 | 1 | 3 |
| α-helix | 260-268 | 9 | |
| β-strand | 273 | 1 | 4 |
| β-strand | 274-278 | 5 | 5 |
| α-helix | 279-287 | 9 | |
| α-helix | 316-318 | 3 | |
| β-strand | 322-331 | 10 | 6 |
| β-strand | 340-349 | 10 | 7 |
| β-strand | 352-353 | 2 | 7 |
| β-strand | 358-359 | 2 | 7 |
| β-strand | 363-364 | 2 | 7 |
| β-strand | 370-380 | 11 | 6 |
| α-helix | 381-383 | 3 | |
| β-strand | 389-397 | 9 | 7 |
| β-strand | 416-424 | 9 | 7 |
| β-strand | 426 | 1 | 8 |
| β-strand | 431 | 1 | 9 |
| β-strand | 432 | 1 | 8 |
| α-helix | 433 | 1 | |
| β-strand | 435-440 | 6 | 6 |
| α-helix | 441 | 1 | |
| β-strand | 442-443 | 2 | 7 |
| α-helix | 444 | 1 | |
| α-helix | 461-462 | 2 | |
| β-strand | 470-475 | 6 | 6 |
| β-strand | 484 | 1 | 9 |
| α-helix | 485-487 | 3 | |
| α-helix | 488-495 | 8 | |
| α-helix | 508-515 | 8 | |
| α-helix | 525-533 | 9 | |
| α-helix | 535-541 | 7 | |
| α-helix | 543-545 | 3 | |
| α-helix | 546-552 | 7 | |
| α-helix | 558-569 | 12 | |
| α-helix | 571-575 | 5 | |
| α-helix | 576-581 | 6 | |
| α-helix | 590-600 | 11 | |
| α-helix | 605-618 | 14 | |
| 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 | 731-732 | 2 | 10 |
| β-strand | 740-741 | 2 | 10 |
| β-strand | 743-744 | 2 | 11 |
| β-strand | 750-751 | 2 | 12 |
| β-strand | 759-762 | 4 | 12 |
| β-strand | 763-764 | 2 | 11 |
| β-strand | 775-780 | 6 | 12 |
| α-helix | 785-803 | 19 | |
| β-strand | 815-819 | 5 | 12 |
| β-strand | 822-826 | 5 | 12 |
| β-strand | 831-833 | 3 | 13 |
| α-helix | 834-837 | 4 | |
| α-helix | 854-862 | 9 | |
| α-helix | 867-889 | 23 | |
| β-strand | 899-902 | 4 | 13 |
| β-strand | 907-909 | 3 | 13 |
| α-helix | 929-932 | 4 | |
| α-helix | 936-942 | 7 | |
| α-helix | 950-969 | 20 | |
| α-helix | 971-981 | 11 | |
| β-strand | 986 | 1 | 14 |
| β-strand | 989 | 1 | 14 |
| α-helix | 992-1001 | 10 | |
| α-helix | 1008-1026 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 442-514 | 73 | |
| α-helix | 518-563 | 46 | |
| α-helix | 567-587 | 21 | |
| α-helix | 591-597 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform | A | protein | 1044 | Homo sapiens | O00329 (AlphaFold model) |
| Phosphatidylinositol 3-kinase regulatory subunit alpha | B | protein | 188 | Bos taurus | P23727 (AlphaFold model) |
>6OCU_1 Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (chains A) MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFH MLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLL IGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGP GTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYT LQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPR AKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSS SEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAW ANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAP HPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQE HFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSL RKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSV ALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMR QEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKN GDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLN KSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIM IRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYC ERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFN EALRESWKTKVNWLAHNVSKDNRQ
>6OCU_2 Phosphatidylinositol 3-kinase regulatory subunit alpha (chains B) MYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEDYTRTSQEIQMKRTAIEAFNE TIKIFEEQCQTQERYSKEYIEKFKREGNETEIQRIMHNYEKLKSRISEIVDSRRRLEEDL KKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNSRACSLEAC GTKLVEKY
| ID | Name | Formula | Copies |
|---|---|---|---|
| M5D | 5-{(3R)-3-methyl-4-[(1R,2R)-2-methylcyclopropane-1-carbonyl]piperazin-1-yl}-3-(… | C19 H23 N7 O | 1 |
Discovery and optimization of heteroaryl piperazines as potent and selective PI3K delta inhibitors. Zhou, H., McGowan, M.A., Lipford, K. et al. Bioorg Med Chem Lett (2020) 30:126715-126715. DOI 10.1016/j.bmcl.2019.126715 · PubMed
Other PDB entries of the same protein (UniProt O00329 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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