Cryo-EM structure of Hsp90:p23 closed-state complex. Determined by electron microscopy at 3.1 Å resolution. Released 25 Aug 2021.
Explore 7L7J in 3D Show helices and sheets RCSB PDB PDBe
7L7J contains 63 α-helices and 70 β-strands across 3 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 | 18-21 | 4 | 4 |
| β-strand | 23-24 | 2 | 5 |
| α-helix | 26-35 | 10 | |
| α-helix | 41-43 | 3 | |
| α-helix | 44-65 | 22 | |
| α-helix | 67-70 | 4 | |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 88-93 | 6 | 6 |
| α-helix | 100-102 | 3 | |
| α-helix | 103-107 | 5 | |
| β-strand | 109-110 | 2 | 7 |
| α-helix | 114-121 | 8 | |
| α-helix | 137-140 | 4 | |
| α-helix | 141-144 | 4 | |
| β-strand | 145-153 | 9 | 6 |
| β-strand | 160-164 | 5 | 6 |
| β-strand | 169-174 | 6 | 6 |
| β-strand | 183-190 | 8 | 6 |
| α-helix | 195-198 | 4 | |
| α-helix | 200-210 | 11 | |
| β-strand | 218-222 | 5 | 6 |
| β-strand | 285-287 | 3 | 6 |
| α-helix | 296-298 | 3 | |
| α-helix | 306-317 | 12 | |
| β-strand | 325-331 | 7 | 8 |
| β-strand | 337-343 | 7 | 8 |
| β-strand | 360-365 | 6 | 8 |
| β-strand | 368-372 | 5 | 8 |
| α-helix | 380-382 | 3 | |
| β-strand | 386-391 | 6 | 8 |
| β-strand | 396 | 1 | 9 |
| β-strand | 403 | 1 | 9 |
| α-helix | 406-427 | 22 | |
| α-helix | 431-451 | 21 | |
| α-helix | 456-459 | 4 | |
| β-strand | 464-465 | 2 | 10 |
| β-strand | 466-467 | 2 | 11 |
| β-strand | 475-476 | 2 | 10 |
| α-helix | 477-483 | 7 | |
| β-strand | 490-495 | 6 | 11 |
| α-helix | 499-503 | 5 | |
| α-helix | 506-508 | 3 | |
| α-helix | 509-514 | 6 | |
| β-strand | 519-521 | 3 | 11 |
| α-helix | 525-532 | 8 | |
| β-strand | 535-536 | 2 | 11 |
| β-strand | 539-543 | 5 | 11 |
| β-strand | 546 | 1 | 12 |
| α-helix | 555-578 | 24 | |
| β-strand | 585-588 | 4 | 12 |
| β-strand | 597-601 | 5 | 12 |
| α-helix | 608-614 | 7 | |
| α-helix | 622-625 | 4 | |
| α-helix | 626-628 | 3 | |
| β-strand | 632-636 | 5 | 12 |
| α-helix | 641-652 | 12 | |
| α-helix | 657-673 | 17 | |
| α-helix | 676-678 | 3 | |
| α-helix | 681-696 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-21 | 4 | 6 |
| β-strand | 23-24 | 2 | 7 |
| α-helix | 26-35 | 10 | |
| α-helix | 41-43 | 3 | |
| α-helix | 44-64 | 21 | |
| α-helix | 67-70 | 4 | |
| β-strand | 78-83 | 6 | 4 |
| β-strand | 88-93 | 6 | 4 |
| α-helix | 100-102 | 3 | |
| α-helix | 103-107 | 5 | |
| β-strand | 109-110 | 2 | 5 |
| α-helix | 114-119 | 6 | |
| α-helix | 137-143 | 7 | |
| β-strand | 145-153 | 9 | 4 |
| β-strand | 159-164 | 6 | 4 |
| β-strand | 169-174 | 6 | 4 |
| β-strand | 183-190 | 8 | 4 |
| α-helix | 192-198 | 7 | |
| α-helix | 200-211 | 12 | |
| β-strand | 218-221 | 4 | 4 |
| β-strand | 286-287 | 2 | 4 |
| α-helix | 296-298 | 3 | |
| α-helix | 306-317 | 12 | |
| β-strand | 323-331 | 9 | 13 |
| β-strand | 337-344 | 8 | 13 |
| β-strand | 361-365 | 5 | 13 |
| β-strand | 368-371 | 4 | 13 |
| α-helix | 380-382 | 3 | |
| β-strand | 386-391 | 6 | 13 |
| β-strand | 396 | 1 | 14 |
| β-strand | 403 | 1 | 14 |
| α-helix | 407-427 | 21 | |
| α-helix | 431-451 | 21 | |
| α-helix | 456-460 | 5 | |
| β-strand | 464-465 | 2 | 15 |
| β-strand | 466-467 | 2 | 16 |
| β-strand | 475-476 | 2 | 15 |
| α-helix | 477-483 | 7 | |
| β-strand | 490-495 | 6 | 16 |
| α-helix | 499-503 | 5 | |
| α-helix | 506-508 | 3 | |
| α-helix | 509-514 | 6 | |
| β-strand | 519-521 | 3 | 16 |
| α-helix | 525-530 | 6 | |
| β-strand | 535-536 | 2 | 16 |
| β-strand | 539-543 | 5 | 16 |
| β-strand | 546 | 1 | 17 |
| α-helix | 555-567 | 13 | |
| α-helix | 569-578 | 10 | |
| β-strand | 585-588 | 4 | 17 |
| β-strand | 597-601 | 5 | 17 |
| α-helix | 602 | 1 | |
| β-strand | 606 | 1 | 18 |
| α-helix | 608-614 | 7 | |
| α-helix | 622-624 | 3 | |
| α-helix | 625-628 | 4 | |
| β-strand | 629 | 1 | 18 |
| α-helix | 630-631 | 2 | |
| β-strand | 632-636 | 5 | 17 |
| α-helix | 641-652 | 12 | |
| α-helix | 657-673 | 17 | |
| α-helix | 676-678 | 3 | |
| α-helix | 681-696 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| β-strand | 6-10 | 5 | 1 |
| β-strand | 14-19 | 6 | 1 |
| β-strand | 25-32 | 8 | 2 |
| β-strand | 35-41 | 7 | 2 |
| β-strand | 48-54 | 7 | 2 |
| β-strand | 55 | 1 | 3 |
| β-strand | 59-68 | 10 | 1 |
| β-strand | 73-79 | 7 | 1 |
| β-strand | 90 | 1 | 3 |
| β-strand | 99-101 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prostaglandin E synthase 3 | C | protein | 160 | Homo sapiens | Q15185 (AlphaFold model) |
| Heat shock protein HSP 90-alpha | A, B | protein | 732 | Homo sapiens | P07900 (AlphaFold model) |
>7L7J_1 Prostaglandin E synthase 3 (chains C) MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCID PNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNF DRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
>7L7J_2 Heat shock protein HSP 90-alpha (chains A, B) MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFME ALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPM GRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKED KEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRN PDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNN IKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKC LELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDY CTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKT LVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIV TSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVK DLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLE GDDDTSRMEEVD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state. Lee, K., Thwin, A.C., Nadel, C.M. et al. Mol Cell (2021) 81:3496. DOI 10.1016/j.molcel.2021.07.023 · PubMed
Other PDB entries of the same protein (UniProt Q15185 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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