2FXS: Yeast HSP82

Name: PDB 2FXS: Yeast HSP82 in complex with the novel HSP90 Inhibitor Radamide
Published: 2007-02-06
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Yeast HSP82 in complex with the novel HSP90 Inhibitor Radamide. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Feb 2007.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,068
Mol. weight: 27.92 kDa
Ligands: RDA
Released: 6 Feb 2007

Explore 2FXS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FXS contains 13 α-helices and 8 β-strands across 1 chain. 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
α-helix	8-9	2
α-helix	10-20	11
α-helix	29-48	20
α-helix	53-56	4
β-strand	64-69	6	1
α-helix	70-72	3
β-strand	74-79	6	1
α-helix	86-90	5
α-helix	91-95	5
α-helix	101-109	9
α-helix	114-120	7
α-helix	123-129	7
β-strand	131-139	9	1
β-strand	146-150	5	1
β-strand	155-160	6	1
α-helix	165-167	3
β-strand	170-177	8	1
α-helix	179-185	7
α-helix	187-197	11
β-strand	205-207	3	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent molecular chaperone HSP82	A	protein	240	Saccharomyces cerevisiae	P02829 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2FXS_1 ATP-dependent molecular chaperone HSP82 (chains A)
MGSSHHHHHHSSGLVPRGSHMASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASD
ALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTL
DEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIP

Ligands and cofactors

ID	Name	Formula	Copies
RDA	Methyl 3-chloro-2-{3-[(2,5-dihydroxy-4-methoxyphenyl)amino]-3-oxopropyl}-4,6-di…	C18 H18 Cl N O8	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. Immormino, R.M., Metzger, L.E., Reardon, P.N. et al. J Mol Biol (2009) 388:1033-1042. DOI 10.1016/j.jmb.2009.03.071 · 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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