Cryo-EM structure of the RAF1-HSP90-CDC37 complex in the closed state. Determined by electron microscopy at 3.7 Å resolution. Released 13 Mar 2024.
Explore 8U1L in 3D Show helices and sheets RCSB PDB PDBe
8U1L contains 74 α-helices and 70 β-strands across 4 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 |
| β-strand | 18-19 | 2 | 2 |
| α-helix | 21-31 | 11 | |
| α-helix | 38-60 | 23 | |
| α-helix | 62-67 | 6 | |
| β-strand | 73-78 | 6 | 3 |
| β-strand | 83-88 | 6 | 3 |
| α-helix | 95-102 | 8 | |
| β-strand | 104-105 | 2 | 4 |
| α-helix | 109-116 | 8 | |
| α-helix | 118 | 1 | |
| α-helix | 132-138 | 7 | |
| β-strand | 140-148 | 9 | 3 |
| β-strand | 154-159 | 6 | 3 |
| β-strand | 164-169 | 6 | 3 |
| β-strand | 178-185 | 8 | 3 |
| α-helix | 187-193 | 7 | |
| α-helix | 195-205 | 11 | |
| β-strand | 213-217 | 5 | 3 |
| β-strand | 220 | 1 | 5 |
| β-strand | 273 | 1 | 5 |
| β-strand | 276-278 | 3 | 3 |
| α-helix | 287-289 | 3 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-308 | 12 | |
| β-strand | 314-322 | 9 | 6 |
| β-strand | 328-335 | 8 | 6 |
| β-strand | 352-356 | 5 | 6 |
| β-strand | 359-362 | 4 | 6 |
| α-helix | 371-373 | 3 | |
| β-strand | 377-382 | 6 | 6 |
| β-strand | 387 | 1 | 7 |
| β-strand | 394 | 1 | 7 |
| α-helix | 398-419 | 22 | |
| α-helix | 422-442 | 21 | |
| α-helix | 447-452 | 6 | |
| β-strand | 455-456 | 2 | 8 |
| β-strand | 458 | 1 | 9 |
| β-strand | 466-467 | 2 | 8 |
| α-helix | 468-472 | 5 | |
| β-strand | 481-486 | 6 | 9 |
| α-helix | 490-494 | 5 | |
| α-helix | 499-504 | 6 | |
| β-strand | 510-512 | 3 | 9 |
| α-helix | 517-523 | 7 | |
| β-strand | 526-527 | 2 | 9 |
| β-strand | 530-534 | 5 | 9 |
| β-strand | 537 | 1 | 10 |
| α-helix | 546-570 | 25 | |
| α-helix | 571-573 | 3 | |
| β-strand | 576-579 | 4 | 11 |
| β-strand | 588-591 | 4 | 11 |
| β-strand | 592 | 1 | 10 |
| α-helix | 599-607 | 9 | |
| α-helix | 613-616 | 4 | |
| α-helix | 617-619 | 3 | |
| α-helix | 620-623 | 4 | |
| β-strand | 624-627 | 4 | 11 |
| α-helix | 632-643 | 12 | |
| α-helix | 648-664 | 17 | |
| α-helix | 667-669 | 3 | |
| α-helix | 672-687 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-16 | 4 | 3 |
| β-strand | 18-19 | 2 | 4 |
| α-helix | 21-30 | 10 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-58 | 20 | |
| α-helix | 62-67 | 6 | |
| β-strand | 73-78 | 6 | 1 |
| β-strand | 83-88 | 6 | 1 |
| α-helix | 95-102 | 8 | |
| β-strand | 104-105 | 2 | 2 |
| α-helix | 109-116 | 8 | |
| α-helix | 118 | 1 | |
| α-helix | 133-138 | 6 | |
| β-strand | 140-148 | 9 | 1 |
| β-strand | 155-159 | 5 | 1 |
| β-strand | 164-169 | 6 | 1 |
| β-strand | 178-185 | 8 | 1 |
| α-helix | 187-193 | 7 | |
| α-helix | 195-205 | 11 | |
| β-strand | 213-218 | 6 | 1 |
| α-helix | 271-272 | 2 | |
| β-strand | 275-278 | 4 | 1 |
| α-helix | 292-294 | 3 | |
| α-helix | 297-308 | 12 | |
| α-helix | 313 | 1 | |
| β-strand | 314-324 | 11 | 12 |
| β-strand | 328-335 | 8 | 12 |
| β-strand | 351-356 | 6 | 12 |
| β-strand | 359-362 | 4 | 12 |
| α-helix | 371-373 | 3 | |
| β-strand | 377-382 | 6 | 12 |
| β-strand | 387 | 1 | 13 |
| β-strand | 394 | 1 | 13 |
| α-helix | 398-418 | 21 | |
| α-helix | 422-442 | 21 | |
| α-helix | 447-451 | 5 | |
| β-strand | 455-456 | 2 | 14 |
| β-strand | 458 | 1 | 15 |
| β-strand | 466-467 | 2 | 14 |
| α-helix | 468-473 | 6 | |
| β-strand | 481-486 | 6 | 15 |
| α-helix | 490-494 | 5 | |
| α-helix | 499-504 | 6 | |
| β-strand | 510-512 | 3 | 15 |
| α-helix | 517-523 | 7 | |
| β-strand | 526-527 | 2 | 15 |
| β-strand | 530-534 | 5 | 15 |
| β-strand | 537 | 1 | 16 |
| α-helix | 546-570 | 25 | |
| β-strand | 576-579 | 4 | 17 |
| β-strand | 588-591 | 4 | 17 |
| β-strand | 592 | 1 | 16 |
| α-helix | 599-607 | 9 | |
| α-helix | 620-623 | 4 | |
| β-strand | 624-627 | 4 | 17 |
| α-helix | 632-643 | 12 | |
| α-helix | 648-664 | 17 | |
| α-helix | 667-669 | 3 | |
| α-helix | 672-687 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 426-428 | 3 | 18 |
| α-helix | 429-431 | 3 | |
| α-helix | 432-436 | 5 | |
| α-helix | 442-461 | 20 | |
| β-strand | 474-477 | 4 | 18 |
| α-helix | 478-480 | 3 | |
| β-strand | 482-484 | 3 | 18 |
| α-helix | 514-517 | 4 | |
| α-helix | 527-543 | 17 | |
| α-helix | 554-563 | 10 | |
| α-helix | 570-572 | 3 | |
| α-helix | 579-588 | 10 | |
| α-helix | 597-598 | 2 | |
| α-helix | 599-611 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10 | 1 | 19 |
| β-strand | 23 | 1 | 18 |
| α-helix | 25-47 | 23 | |
| α-helix | 103-111 | 9 | |
| α-helix | 113 | 1 | |
| β-strand | 114 | 1 | 19 |
| α-helix | 116-119 | 4 | |
| β-strand | 120-123 | 4 | 12 |
| β-strand | 127-129 | 3 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein 83 | A, B | protein | 722 | Trichoplusia ni | A0A7E5VSK5 (AlphaFold model) |
| RAF proto-oncogene serine/threonine-protein kinase | C | protein | 656 | Homo sapiens | P04049 (AlphaFold model) |
| Hsp90 co-chaperone Cdc37, N-terminally processed | D | protein | 378 | Homo sapiens | Q16543 (AlphaFold model) |
>8U1L_1 Heat shock protein 83 (chains A, B) MPEEMQTDSGEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT DPSKLDSGKELYIKIIPNKSEGTFTIIDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAG ADISMIGQFGVGFYSCYLVADRVTVHSKHNDDEQYMWESSAGGSFTVRTDHGEPLGRGTK IVLHIKEDLAEYLEVNKIKEIVKKHSQFIGYPIKLTVEKEREKELAYDEEEEKKEGEEDK KEDEKEDEKPKIEDVGEDDEEDKDKKKKKTIKEKYTEDEELNKTKPIWTRNADDITQEEY GDFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENKKRKNNIKLYVRRVF IMDNCEDLIPEYLNFIKGVVDSEDLPLNISREMLQQNKILKVIRKNLVKKCLELFEELAE DKENYKKYYEQFSKNLKLGIHEDAQNRTKLADLLRYHTSASGDEACSLKEYVSRMKENQK HIYYITGENRDQVANSSFVERVKKRGYEVVYMTEPIDEYVVQQMREYDGKTLVSVTKEGL ELPEDEEEKKKREEDKVKFEGLCKVMKNILDNKVEKVVVSNRLVESPCCIVTAQYGWSAN MERIMKAQALRDTSTMGYMAAKKHLEINPDHSIVETLRQKAEADKNDKAVKDLVILLYET ALLSSGFTLDEPQVHASRIYRMIKLGLGIDEDEPIQVEESSVGDVPPLEGDADDASRMEE VD
>8U1L_2 RAF proto-oncogene serine/threonine-protein kinase (chains C) GGEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIR VFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAA SLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTK VPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFT FNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNN LSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGS FGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI VTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG LTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLY ELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLF PQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVFGHHHHHH
>8U1L_3 Hsp90 co-chaperone Cdc37, N-terminally processed (chains D) MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDVSV
Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural elements. Finci, L.I., Chakrabarti, M., Gulten, G. et al. Commun Biol (2024) 7:260-260. DOI 10.1038/s42003-024-05959-3 · PubMed
Other PDB entries of the same protein (UniProt A0A7E5VSK5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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