Crystal structure of the Arabidopsis thaliana Raptor in complex with the TOS peptide of human PRAS40. Determined by X-ray diffraction at 3.35 Å resolution. Released 20 Dec 2017.
Explore 5WBL in 3D Show helices and sheets RCSB PDB PDBe
5WBL contains 42 α-helices and 42 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 |
|---|---|---|---|
| α-helix | 62-64 | 3 | |
| α-helix | 76-78 | 3 | |
| α-helix | 90-91 | 2 | |
| β-strand | 106-114 | 9 | 1 |
| β-strand | 134 | 1 | 2 |
| β-strand | 137 | 1 | 2 |
| α-helix | 144-160 | 17 | |
| β-strand | 167-172 | 6 | 1 |
| β-strand | 175 | 1 | 3 |
| α-helix | 176-189 | 14 | |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 205-208 | 4 | |
| β-strand | 212-216 | 5 | 3 |
| β-strand | 223-227 | 5 | 3 |
| α-helix | 228-234 | 7 | |
| β-strand | 239-244 | 6 | 1 |
| α-helix | 249-257 | 9 | |
| β-strand | 273-277 | 5 | 1 |
| α-helix | 295-301 | 7 | |
| α-helix | 303-314 | 12 | |
| α-helix | 323-325 | 3 | |
| α-helix | 339-358 | 20 | |
| α-helix | 361-368 | 8 | |
| α-helix | 372-390 | 19 | |
| β-strand | 396-397 | 2 | 1 |
| α-helix | 410-429 | 20 | |
| α-helix | 436-438 | 3 | |
| α-helix | 440-453 | 14 | |
| α-helix | 465-471 | 7 | |
| α-helix | 478-489 | 12 | |
| α-helix | 493-502 | 10 | |
| α-helix | 505-510 | 6 | |
| α-helix | 511-513 | 3 | |
| α-helix | 517-533 | 17 | |
| α-helix | 535-537 | 3 | |
| α-helix | 538-543 | 6 | |
| α-helix | 547-555 | 9 | |
| α-helix | 561-575 | 15 | |
| α-helix | 579-587 | 9 | |
| α-helix | 590-597 | 8 | |
| α-helix | 610-624 | 15 | |
| α-helix | 628-635 | 8 | |
| α-helix | 639-643 | 5 | |
| α-helix | 644-648 | 5 | |
| α-helix | 652-664 | 13 | |
| α-helix | 685-698 | 14 | |
| α-helix | 706-722 | 17 | |
| α-helix | 724-734 | 11 | |
| α-helix | 833-844 | 12 | |
| α-helix | 849-862 | 14 | |
| α-helix | 958-960 | 3 | |
| α-helix | 966-971 | 6 | |
| α-helix | 986-1008 | 23 | |
| β-strand | 1015-1023 | 9 | 4 |
| β-strand | 1032-1035 | 4 | 5 |
| β-strand | 1041-1045 | 5 | 5 |
| β-strand | 1051-1055 | 5 | 5 |
| β-strand | 1061 | 1 | 5 |
| β-strand | 1075-1081 | 7 | 6 |
| β-strand | 1088-1093 | 6 | 6 |
| β-strand | 1097-1101 | 5 | 6 |
| β-strand | 1112-1117 | 6 | 6 |
| β-strand | 1132-1136 | 5 | 7 |
| β-strand | 1141-1145 | 5 | 7 |
| β-strand | 1150-1155 | 6 | 7 |
| β-strand | 1160-1166 | 7 | 7 |
| β-strand | 1173-1178 | 6 | 8 |
| β-strand | 1185-1190 | 6 | 8 |
| β-strand | 1195-1199 | 5 | 8 |
| β-strand | 1206-1210 | 5 | 8 |
| β-strand | 1221 | 1 | 9 |
| β-strand | 1224 | 1 | 10 |
| β-strand | 1231-1232 | 2 | 10 |
| β-strand | 1236 | 1 | 9 |
| β-strand | 1241-1244 | 4 | 9 |
| β-strand | 1245-1246 | 2 | 10 |
| β-strand | 1255-1258 | 4 | 9 |
| β-strand | 1264-1269 | 6 | 11 |
| β-strand | 1275-1280 | 6 | 11 |
| β-strand | 1284-1289 | 6 | 11 |
| β-strand | 1294-1299 | 6 | 11 |
| β-strand | 1314-1317 | 4 | 4 |
| β-strand | 1324-1327 | 4 | 4 |
| β-strand | 1332-1337 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulatory-associated protein of TOR 1 | A | protein | 1287 | Arabidopsis thaliana | Q93YQ1 (AlphaFold model) |
| Proline-rich AKT1 substrate 1 | T | protein | 16 | Homo sapiens | Q96B36 (AlphaFold model) |
>5WBL_1 Regulatory-associated protein of TOR 1 (chains A) SVDMALGDLMVSRFSQSSVSLVSNHRYDEDCVSSHDDGDSRRKDSEAKSSSSYGNGTTEG AATATSMAYLPQTIVLCELRHDASEASAPLGTSEIVLVPKWRLKERMKTGCVALVLCLNI TVDPPDVIKISPCARIEAWIDPFSMAPPKALETIGKNLSTQYERWQPRARYKVQLDPTVD EVRKLCLTCRKYAKTERVLFHYNGHGVPKPTANGEIWVFNKSYTQYIPLPISELDSWLKT PSIYVFDCSAARMILNAFAELHDWGSSGSSGSSRDCILLAACDVHETLPQSVEFPADVFT SCLTTPIKMALKWFCRRSLLKEIIDESLIDRIPGRQNDRKTLLGELNWIFTAVTDTIAWN VLPHELFQRLFRQDLLVASLFRNFLLAERIMRSANCNPISHPMLPPTHQHHMWDAWDMAA EICLSQLPQLVLDPSTEFQPSPFFTEQLTAFEVWLDHGSEHKKPPEQLPIVLQVLLSQCH RFRALVLLGRFLDMGSWAVDLALSVGIFPYVLKLLQTTTNELRQILVFIWTKILALDKSC QIDLVKDGGHTYFIRFLDSSGAFPEQRAMAAFVLAVIVDGHRRGQEACLEANLIGVCLGH LEASRPSDPQPEPLFLQWLCLCLGKLWEDFMEAQIMGREANAFEKLAPLLSEPQPEVRAA AVFALGTLLDIGFDSNKSVVEDEFDDDEKIRAEDAIIKSLLDVVSDGSPLVRAEVAVALA RFAFGHKQHLKLAAASYWKPQSSSLLTSLPSIAKFHDPGSATIVSLHMSPLTRASTDSQP VARESRISSSPLGSSGLMQGSPLSDDSSLHSDSGMMHDSVSNGAVHQPRLLDNAVYSQCV RAMFALAKDPSPRIASLGRRVLSIIGIEQVVAKPSKPTGRPGEAADSGLADPLLGASGSE RSLLPLSTIYGWSCGHFSKPLLGGADASQEIAAKREEKEKFALEHIAKCQHSSISKLNNN PIANWDTRFETGTKTALLHPFSPIVVAADENERIRVWNYEEATLLNGFDNHDFPDKGISK LCLINELDDSLLLVASCDGSVRIWKNYATKGKQKLVTGFSSIQGHKPGARDLNAVVDWQQ QSGYLYASGETSTVTLWDLEKEQLVRSVPSESECGVTALSASQVHGGQLAAGFADGSLRL YDVRSPEPLVCATRPHQKVERVVGLSFQPGLDPAKVVSASQAGDIQFLDLRTTRDTYLTI DAHRGSLTALAVHRHAPIIASGSAKQLIKVFSLQGEQLGIIRYYPSFMAQKIGSVSCLTF HPYQVLLAAGAADSFVSIYTHDNSQAR
>5WBL_2 Proline-rich AKT1 substrate 1 (chains T) DNGGLFVMDEDATLQD
Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40. Yang, H., Jiang, X., Li, B. et al. Nature (2017) 552:368-373. DOI 10.1038/nature25023 · PubMed
Other PDB entries of the same protein (UniProt Q93YQ1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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