Cryo-EM structure of the cross-linked HSP90 dimer (NTD-MD) in the semi-open state. Determined by electron microscopy at 3.9 Å resolution. Released 13 Mar 2024.
Explore 8U1N in 3D Show helices and sheets RCSB PDB PDBe
8U1N contains 38 α-helices and 52 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 | 12-16 | 5 | 1 |
| β-strand | 18-19 | 2 | 2 |
| α-helix | 22-31 | 10 | |
| α-helix | 39-60 | 22 | |
| α-helix | 62-67 | 6 | |
| β-strand | 73-75 | 3 | 3 |
| β-strand | 78 | 1 | 3 |
| β-strand | 83-88 | 6 | 3 |
| α-helix | 95-97 | 3 | |
| α-helix | 98-102 | 5 | |
| β-strand | 104-105 | 2 | 4 |
| α-helix | 109-116 | 8 | |
| α-helix | 133-138 | 6 | |
| 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 | 213-215 | 3 | 3 |
| α-helix | 297-307 | 11 | |
| β-strand | 314-322 | 9 | 5 |
| β-strand | 328-335 | 8 | 5 |
| β-strand | 352-354 | 3 | 5 |
| β-strand | 355 | 1 | 6 |
| β-strand | 360 | 1 | 6 |
| α-helix | 371-373 | 3 | |
| β-strand | 377-382 | 6 | 5 |
| β-strand | 387 | 1 | 7 |
| β-strand | 394 | 1 | 7 |
| α-helix | 398-420 | 23 | |
| α-helix | 422-442 | 21 | |
| α-helix | 447-451 | 5 | |
| β-strand | 455-456 | 2 | 8 |
| β-strand | 458 | 1 | 9 |
| β-strand | 466-467 | 2 | 8 |
| α-helix | 468-471 | 4 | |
| α-helix | 472-474 | 3 | |
| β-strand | 483-485 | 3 | 9 |
| α-helix | 492-495 | 4 | |
| α-helix | 502-504 | 3 | |
| β-strand | 509-511 | 3 | 9 |
| α-helix | 517-523 | 7 | |
| β-strand | 527 | 1 | 10 |
| β-strand | 530 | 1 | 10 |
| β-strand | 533-534 | 2 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-16 | 4 | 3 |
| β-strand | 18-19 | 2 | 4 |
| α-helix | 21-31 | 11 | |
| α-helix | 39-60 | 22 | |
| β-strand | 73-77 | 5 | 1 |
| β-strand | 83-88 | 6 | 1 |
| α-helix | 95-96 | 2 | |
| α-helix | 97-101 | 5 | |
| β-strand | 104-105 | 2 | 2 |
| α-helix | 109-114 | 6 | |
| α-helix | 133-138 | 6 | |
| β-strand | 140-148 | 9 | 1 |
| β-strand | 154-159 | 6 | 1 |
| β-strand | 164-169 | 6 | 1 |
| β-strand | 178-185 | 8 | 1 |
| α-helix | 190-193 | 4 | |
| α-helix | 195-205 | 11 | |
| β-strand | 213 | 1 | 1 |
| α-helix | 269-271 | 3 | |
| α-helix | 297-308 | 12 | |
| β-strand | 317-322 | 6 | 11 |
| β-strand | 328-333 | 6 | 11 |
| β-strand | 352-356 | 5 | 11 |
| β-strand | 360-362 | 3 | 11 |
| α-helix | 371-373 | 3 | |
| β-strand | 377-382 | 6 | 11 |
| α-helix | 397-417 | 21 | |
| α-helix | 418-420 | 3 | |
| α-helix | 422-442 | 21 | |
| α-helix | 447-453 | 7 | |
| β-strand | 455-456 | 2 | 12 |
| β-strand | 457 | 1 | 13 |
| β-strand | 466-467 | 2 | 12 |
| α-helix | 468-473 | 6 | |
| β-strand | 482-483 | 2 | 14 |
| β-strand | 484 | 1 | 15 |
| α-helix | 490-494 | 5 | |
| α-helix | 497-503 | 7 | |
| β-strand | 510 | 1 | 15 |
| β-strand | 511 | 1 | 13 |
| α-helix | 515-520 | 6 | |
| β-strand | 526-527 | 2 | 16 |
| β-strand | 530-531 | 2 | 16 |
| β-strand | 532-533 | 2 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein 83 | A, B | protein | 722 | Trichoplusia ni | A0A7E5VSK5 (AlphaFold model) |
>8U1N_1 Heat shock protein 83 (chains A, B) MPEEMQTDSGEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT DPSKLDSGKELYIKIIPNKSEGTFTIIDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAG ADISMIGQFGVGFYSCYLVADRVTVHSKHNDDEQYMWESSAGGSFTVRTDHGEPLGRGTK IVLHIKEDLAEYLEVNKIKEIVKKHSQFIGYPIKLTVEKEREKELAYDEEEEKKEGEEDK KEDEKEDEKPKIEDVGEDDEEDKDKKKKKTIKEKYTEDEELNKTKPIWTRNADDITQEEY GDFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENKKRKNNIKLYVRRVF IMDNCEDLIPEYLNFIKGVVDSEDLPLNISREMLQQNKILKVIRKNLVKKCLELFEELAE DKENYKKYYEQFSKNLKLGIHEDAQNRTKLADLLRYHTSASGDEACSLKEYVSRMKENQK HIYYITGENRDQVANSSFVERVKKRGYEVVYMTEPIDEYVVQQMREYDGKTLVSVTKEGL ELPEDEEEKKKREEDKVKFEGLCKVMKNILDNKVEKVVVSNRLVESPCCIVTAQYGWSAN MERIMKAQALRDTSTMGYMAAKKHLEINPDHSIVETLRQKAEADKNDKAVKDLVILLYET ALLSSGFTLDEPQVHASRIYRMIKLGLGIDEDEPIQVEESSVGDVPPLEGDADDASRMEE VD
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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