Structure of the RAF1-HSP90-CDC37 complex (RHC-I). Determined by electron microscopy at 3.16 Å resolution. Released 14 Sept 2022.
Explore 7Z38 in 3D Show helices and sheets RCSB PDB PDBe
7Z38 contains 76 α-helices and 68 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 | 14-16 | 3 | 1 |
| β-strand | 18-19 | 2 | 2 |
| α-helix | 21-30 | 10 | |
| α-helix | 38-60 | 23 | |
| α-helix | 62-65 | 4 | |
| β-strand | 73-78 | 6 | 3 |
| β-strand | 83-88 | 6 | 3 |
| α-helix | 95-100 | 6 | |
| β-strand | 104-105 | 2 | 4 |
| α-helix | 109-117 | 9 | |
| α-helix | 132-138 | 7 | |
| β-strand | 140-148 | 9 | 3 |
| β-strand | 155-159 | 5 | 3 |
| β-strand | 164-168 | 5 | 3 |
| β-strand | 178-185 | 8 | 3 |
| α-helix | 190-193 | 4 | |
| α-helix | 195-204 | 10 | |
| β-strand | 213-217 | 5 | 3 |
| β-strand | 222 | 1 | 5 |
| β-strand | 271 | 1 | 5 |
| β-strand | 277-279 | 3 | 3 |
| α-helix | 281-283 | 3 | |
| α-helix | 288-290 | 3 | |
| 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 | 360-363 | 4 | 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 | 456-457 | 2 | 8 |
| β-strand | 459 | 1 | 9 |
| β-strand | 467-468 | 2 | 8 |
| α-helix | 469-475 | 7 | |
| β-strand | 483-487 | 5 | 9 |
| α-helix | 491-495 | 5 | |
| α-helix | 501-505 | 5 | |
| β-strand | 510-513 | 4 | 9 |
| α-helix | 517-524 | 8 | |
| β-strand | 527-528 | 2 | 10 |
| β-strand | 531-532 | 2 | 10 |
| β-strand | 533-535 | 3 | 9 |
| β-strand | 538 | 1 | 11 |
| α-helix | 547-559 | 13 | |
| α-helix | 562-570 | 9 | |
| β-strand | 577-580 | 4 | 11 |
| β-strand | 589-593 | 5 | 11 |
| α-helix | 594 | 1 | |
| α-helix | 600-607 | 8 | |
| α-helix | 614-616 | 3 | |
| β-strand | 624-628 | 5 | 11 |
| α-helix | 633-644 | 12 | |
| α-helix | 649-665 | 17 | |
| α-helix | 673-688 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-16 | 3 | 3 |
| β-strand | 18-19 | 2 | 4 |
| α-helix | 21-30 | 10 | |
| α-helix | 38-60 | 23 | |
| α-helix | 62-65 | 4 | |
| β-strand | 73-78 | 6 | 1 |
| β-strand | 83-88 | 6 | 1 |
| α-helix | 95-100 | 6 | |
| β-strand | 104-105 | 2 | 2 |
| α-helix | 109-114 | 6 | |
| α-helix | 132-138 | 7 | |
| β-strand | 140-148 | 9 | 1 |
| β-strand | 155-159 | 5 | 1 |
| β-strand | 164-168 | 5 | 1 |
| β-strand | 178-185 | 8 | 1 |
| α-helix | 190-193 | 4 | |
| α-helix | 195-204 | 10 | |
| β-strand | 213-218 | 6 | 1 |
| β-strand | 276-279 | 4 | 1 |
| α-helix | 280-283 | 4 | |
| α-helix | 288-290 | 3 | |
| α-helix | 298-309 | 12 | |
| β-strand | 317-323 | 7 | 12 |
| β-strand | 329-335 | 7 | 12 |
| α-helix | 346-348 | 3 | |
| β-strand | 353-357 | 5 | 12 |
| β-strand | 360-364 | 5 | 12 |
| α-helix | 372-374 | 3 | |
| β-strand | 378-383 | 6 | 12 |
| β-strand | 388 | 1 | 13 |
| β-strand | 395 | 1 | 13 |
| α-helix | 400-420 | 21 | |
| α-helix | 423-443 | 21 | |
| α-helix | 448-452 | 5 | |
| β-strand | 456-457 | 2 | 14 |
| β-strand | 458 | 1 | 15 |
| β-strand | 467-468 | 2 | 14 |
| α-helix | 469-475 | 7 | |
| β-strand | 482-487 | 6 | 15 |
| α-helix | 491-495 | 5 | |
| α-helix | 498-500 | 3 | |
| α-helix | 501-505 | 5 | |
| β-strand | 511-513 | 3 | 15 |
| α-helix | 516-524 | 9 | |
| β-strand | 532-535 | 4 | 15 |
| β-strand | 538 | 1 | 16 |
| α-helix | 547-570 | 24 | |
| β-strand | 577-579 | 3 | 17 |
| β-strand | 589-592 | 4 | 17 |
| β-strand | 593 | 1 | 16 |
| α-helix | 600-606 | 7 | |
| β-strand | 625-628 | 4 | 17 |
| α-helix | 633-644 | 12 | |
| α-helix | 649-666 | 18 | |
| α-helix | 668-670 | 3 | |
| α-helix | 673-688 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 429-430 | 2 | 18 |
| α-helix | 442-461 | 20 | |
| α-helix | 471-473 | 3 | |
| β-strand | 475-476 | 2 | 18 |
| β-strand | 482-483 | 2 | 18 |
| α-helix | 514-518 | 5 | |
| α-helix | 527-542 | 16 | |
| α-helix | 554-563 | 10 | |
| α-helix | 573-574 | 2 | |
| α-helix | 580-588 | 9 | |
| α-helix | 597-598 | 2 | |
| α-helix | 599-611 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10 | 1 | 19 |
| α-helix | 25-73 | 49 | |
| α-helix | 78-111 | 34 | |
| β-strand | 114 | 1 | 19 |
| α-helix | 116-119 | 4 | |
| β-strand | 120-122 | 3 | 6 |
| β-strand | 126-129 | 4 | 6 |
| α-helix | 143-154 | 12 | |
| α-helix | 156-164 | 9 | |
| α-helix | 168-177 | 10 | |
| α-helix | 179-181 | 3 | |
| α-helix | 184-200 | 17 | |
| α-helix | 203-226 | 24 | |
| α-helix | 230-242 | 13 | |
| α-helix | 246-273 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein HSP 90-beta | A, B | protein | 732 | Homo sapiens | P08238 (AlphaFold model) |
| RAF proto-oncogene serine/threonine-protein kinase | C | protein | 659 | Homo sapiens | P04049 (AlphaFold model) |
| Hsp90 co-chaperone Cdc37 | D | protein | 394 | Homo sapiens | Q16543 (AlphaFold model) |
>7Z38_1 Heat shock protein HSP 90-beta (chains A, B) MYPYDVPDYAEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALD KIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKA FMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHG EPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEE EKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRN PDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNN IKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKC LELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEY VSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKS LVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIV TSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVK DLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLE GDEDASRMEEVD
>7Z38_2 RAF proto-oncogene serine/threonine-protein kinase (chains C) MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRV FLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAAS LIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKV PTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTF NTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNL SPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSF GTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAVI TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL TVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYE LMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFP QILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVFGSAWSHPQFEK
>7Z38_3 Hsp90 co-chaperone Cdc37 (chains D) MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDVSVTRTRPLEQKLISEEDL
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:
MolViewer shows 7Z38 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.