9Q8O: Hsp82-MD

Name: PDB 9Q8O: Crystal structure of Hsp82-MD in complex with the CS domain of Sgt1
Published: 2026-01-21
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of Hsp82-MD in complex with the CS domain of Sgt1. Determined by X-ray diffraction at 2.1 Å resolution. Released 21 Jan 2026.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 2,975
Mol. weight: 41.09 kDa
Released: 21 Jan 2026

Explore 9Q8O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q8O contains 14 α-helices and 19 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.

Chain A: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	276-278	3
α-helix	281-283	3
α-helix	286-297	12
β-strand	305-313	9	1
β-strand	317-323	7	1
β-strand	341-345	5	1
β-strand	348-351	4	1
α-helix	360-362	3
β-strand	366-371	6	1
α-helix	374-375	2
α-helix	380-384	5
α-helix	387-408	22
α-helix	411-431	21
α-helix	436-440	5
β-strand	444-447	4	2
β-strand	450-456	7	2
α-helix	457-463	7
β-strand	471-475	5	2
α-helix	479-483	5
α-helix	488-494	7
β-strand	498-501	4	2
α-helix	504-513	10
β-strand	515-516	2	3
β-strand	519-520	2	3
β-strand	521-523	3	2

Chain B: 1 helix, 7 β-strands

Element	Residues	Length	Sheet
β-strand	153-158	6	4
β-strand	162-168	7	4
α-helix	176-178	3
β-strand	180-183	4	1
β-strand	190-197	8	1
β-strand	202-209	8	1
β-strand	214-223	10	4
β-strand	228-234	7	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent molecular chaperone HSP82	A	protein	257	Saccharomyces cerevisiae	P02829 (AlphaFold model)
Protein SGT1	B	protein	94	Saccharomyces cerevisiae	Q08446 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9Q8O_1 ATP-dependent molecular chaperone HSP82 (chains A)
TKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLF
ESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVI
RKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVD
ELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQ
LKEFEGKTLVDITKDFE

Sequence of entity 2 (B), FASTA

>9Q8O_2 Protein SGT1 (chains B)
KFKIDWYQSSTSVTISLFTVNLPESKEQVNIYISPNDRRTLSISYQVPKSGSEFQYNAKL
SHEVDPKAVSLKIFPKKLEITLSKIDSTQWKKLE

Primary citation

The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle. Engler, S., Delhommel, F., Dodt, C. et al. Mol Cell (2026) 86:166-179.e6. DOI 10.1016/j.molcel.2025.12.002 · PubMed

Other PDB entries of the same protein (UniProt P02829 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2IWX 1.5 Å, Analogues of radicicol bound to the ATP-binding site of Hsp90.
2BRC 1.6 Å, Structure of a Hsp90 Inhibitor bound to the N-terminus of Yeast Hsp90.
2WER 1.6 Å, Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol
3C11 1.6 Å, Yeast Hsp82 N-terminal domain-Geldanamycin complex: effects of mutants 98-99 KS-AA
1ZWH 1.65 Å, Yeast Hsp82 in complex with the novel Hsp90 inhibitor Radester amine
1AH6 1.8 Å, Structure of the tetragonal form of the N-terminal domain of the yeast HSP90 chaperone
1AMW 1.85 Å, ADP binding site in the HSP90 molecular chaperone
2XX2 1.85 Å, Macrolactone Inhibitor bound to HSP90 N-term
1ZW9 1.9 Å, Yeast HSP82 in complex with the Novel HSP90 Inhibitor 8-(6-Bromo-benzo[1,3]dioxol-5-ylsul…
2VW5 1.9 Å, Structure Of The Hsp90 Inhibitor 7-O-carbamoylpremacbecin Bound To The N- Terminus Of…
3C0E 1.9 Å, Yeast Hsp82 N-terminal domain: effects of mutants 98-99 KS-AA
2AKP 1.94 Å, Hsp90 Delta24-N210 mutant

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