Structure of the RAF1-HSP90-CDC37 complex (RHC-II). Determined by electron microscopy at 3.67 Å resolution. Released 14 Sept 2022.
Explore 7Z37 in 3D Show helices and sheets RCSB PDB PDBe
7Z37 contains 78 α-helices and 67 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 | 12-14 | 3 | 1 |
| β-strand | 18-19 | 2 | 2 |
| α-helix | 21-29 | 9 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-60 | 22 | |
| α-helix | 62-65 | 4 | |
| β-strand | 73-78 | 6 | 3 |
| β-strand | 83-88 | 6 | 3 |
| α-helix | 95-103 | 9 | |
| β-strand | 104-105 | 2 | 4 |
| α-helix | 109-117 | 9 | |
| α-helix | 133-138 | 6 | |
| β-strand | 140-148 | 9 | 3 |
| β-strand | 155-159 | 5 | 3 |
| β-strand | 165-167 | 3 | 3 |
| β-strand | 169 | 1 | 3 |
| β-strand | 178-185 | 8 | 3 |
| α-helix | 187-193 | 7 | |
| α-helix | 195-204 | 10 | |
| β-strand | 213-215 | 3 | 3 |
| β-strand | 217-222 | 6 | 5 |
| β-strand | 272-277 | 6 | 5 |
| α-helix | 293-295 | 3 | |
| α-helix | 298-309 | 12 | |
| β-strand | 315-325 | 11 | 6 |
| β-strand | 329-336 | 8 | 6 |
| α-helix | 346-348 | 3 | |
| β-strand | 353-357 | 5 | 6 |
| β-strand | 361-363 | 3 | 6 |
| α-helix | 372-374 | 3 | |
| β-strand | 378-383 | 6 | 6 |
| β-strand | 388 | 1 | 7 |
| β-strand | 395 | 1 | 7 |
| α-helix | 399-419 | 21 | |
| α-helix | 423-443 | 21 | |
| α-helix | 448-452 | 5 | |
| β-strand | 457-458 | 2 | 8 |
| β-strand | 459 | 1 | 9 |
| α-helix | 460-462 | 3 | |
| β-strand | 466-467 | 2 | 8 |
| α-helix | 469-475 | 7 | |
| β-strand | 482-487 | 6 | 9 |
| α-helix | 491-495 | 5 | |
| α-helix | 501-505 | 5 | |
| β-strand | 511-513 | 3 | 9 |
| α-helix | 516-521 | 6 | |
| β-strand | 527-528 | 2 | 9 |
| β-strand | 531-535 | 5 | 9 |
| β-strand | 538 | 1 | 10 |
| α-helix | 547-559 | 13 | |
| α-helix | 562-570 | 9 | |
| β-strand | 578-579 | 2 | 10 |
| β-strand | 589-593 | 5 | 10 |
| α-helix | 600-607 | 8 | |
| β-strand | 624-628 | 5 | 10 |
| α-helix | 633-644 | 12 | |
| α-helix | 649-665 | 17 | |
| α-helix | 668-670 | 3 | |
| α-helix | 673-688 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-14 | 2 | 3 |
| β-strand | 18-19 | 2 | 4 |
| α-helix | 21-30 | 10 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-60 | 22 | |
| α-helix | 62-64 | 3 | |
| β-strand | 73-78 | 6 | 1 |
| β-strand | 83-88 | 6 | 1 |
| α-helix | 95-101 | 7 | |
| β-strand | 104-105 | 2 | 2 |
| α-helix | 109-115 | 7 | |
| α-helix | 133-138 | 6 | |
| β-strand | 140-148 | 9 | 1 |
| β-strand | 155-159 | 5 | 1 |
| β-strand | 166-168 | 3 | 1 |
| β-strand | 178-185 | 8 | 1 |
| α-helix | 190-192 | 3 | |
| α-helix | 195-204 | 10 | |
| α-helix | 212 | 1 | |
| β-strand | 213-218 | 6 | 1 |
| β-strand | 276-279 | 4 | 1 |
| α-helix | 298-308 | 11 | |
| β-strand | 317-323 | 7 | 11 |
| β-strand | 329-335 | 7 | 11 |
| α-helix | 346-348 | 3 | |
| β-strand | 353-357 | 5 | 11 |
| β-strand | 360-363 | 4 | 11 |
| α-helix | 372-374 | 3 | |
| β-strand | 378-383 | 6 | 11 |
| α-helix | 387 | 1 | |
| β-strand | 388 | 1 | 12 |
| α-helix | 389 | 1 | |
| β-strand | 395 | 1 | 12 |
| α-helix | 398-400 | 3 | |
| α-helix | 401-419 | 19 | |
| α-helix | 423-443 | 21 | |
| α-helix | 448-452 | 5 | |
| β-strand | 456-457 | 2 | 13 |
| β-strand | 458-459 | 2 | 14 |
| β-strand | 467-468 | 2 | 13 |
| α-helix | 469-474 | 6 | |
| β-strand | 482-487 | 6 | 14 |
| α-helix | 491-495 | 5 | |
| α-helix | 501-505 | 5 | |
| β-strand | 510-513 | 4 | 14 |
| α-helix | 517-524 | 8 | |
| β-strand | 528 | 1 | 15 |
| β-strand | 531 | 1 | 15 |
| β-strand | 532-535 | 4 | 14 |
| β-strand | 538 | 1 | 16 |
| α-helix | 547-570 | 24 | |
| β-strand | 577-580 | 4 | 17 |
| β-strand | 589-592 | 4 | 17 |
| β-strand | 593 | 1 | 16 |
| α-helix | 600-607 | 8 | |
| β-strand | 625-628 | 4 | 17 |
| α-helix | 633-644 | 12 | |
| α-helix | 649-665 | 17 | |
| α-helix | 673-688 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 433-436 | 4 | |
| α-helix | 442-461 | 20 | |
| α-helix | 471-473 | 3 | |
| β-strand | 475-477 | 3 | 18 |
| β-strand | 481-483 | 3 | 18 |
| α-helix | 514-518 | 5 | |
| α-helix | 527-543 | 17 | |
| α-helix | 554-563 | 10 | |
| α-helix | 573-574 | 2 | |
| α-helix | 580-588 | 9 | |
| α-helix | 599-611 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10 | 1 | 19 |
| α-helix | 25-73 | 49 | |
| α-helix | 78-111 | 34 | |
| α-helix | 113 | 1 | |
| β-strand | 114 | 1 | 19 |
| α-helix | 116-119 | 4 | |
| β-strand | 120-129 | 10 | 6 |
| α-helix | 142-154 | 13 | |
| α-helix | 156-163 | 8 | |
| α-helix | 168-177 | 10 | |
| α-helix | 179-181 | 3 | |
| α-helix | 184-199 | 16 | |
| α-helix | 203-226 | 24 | |
| α-helix | 230-232 | 3 | |
| α-helix | 235-242 | 8 | |
| α-helix | 246-273 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein HSP 90-beta | AP1, BP1 | protein | 732 | Homo sapiens | P08238 (AlphaFold model) |
| RAF proto-oncogene serine/threonine-protein kinase | CP1 | protein | 659 | Homo sapiens | P04049 (AlphaFold model) |
| Hsp90 co-chaperone Cdc37 | DP1 | protein | 394 | Homo sapiens | Q16543 (AlphaFold model) |
>7Z37_1 Heat shock protein HSP 90-beta (chains AP1, BP1) MYPYDVPDYAEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALD KIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKA FMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHG EPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEE EKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRN PDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNN IKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKC LELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEY VSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKS LVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIV TSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVK DLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLE GDEDASRMEEVD
>7Z37_2 RAF proto-oncogene serine/threonine-protein kinase (chains CP1) MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRV FLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAAS LIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKV PTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTF NTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNL SPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSF GTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAVI TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL TVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYE LMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFP QILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVFGSAWSHPQFEK
>7Z37_3 Hsp90 co-chaperone Cdc37 (chains DP1) MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDVSVTRTRPLEQKLISEEDL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 2 |
Structure of the RAF1-HSP90-CDC37 complex reveals the basis of RAF1 regulation. Garcia-Alonso, S., Mesa, P., Ovejero, L.P. et al. Mol Cell (2022) 82:3438-3452.e8. DOI 10.1016/j.molcel.2022.08.012 · PubMed
Other PDB entries of the same protein (UniProt P08238 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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