2WER: ATP-dependent molecular chaperone HSP82

Name: PDB 2WER: Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol
Published: 2009-04-14
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol. Determined by X-ray diffraction at 1.6 Å resolution. Released 14 Apr 2009.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 2
Atoms: 3,860
Mol. weight: 50.45 kDa
Ligands: RDC
Released: 14 Apr 2009

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

Secondary structure: helices and β-sheets

2WER contains 24 α-helices and 16 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.

Chains A and B: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
α-helix	8-9	2
α-helix	10-20	11
α-helix	29-49	21
α-helix	53-58	6
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	101-108	8
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
β-strand	170-177	8	1
α-helix	182-185	4
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, B	protein	220	SACCHAROMYCES CEREVISIAE	P02829 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2WER_1 ATP-DEPENDENT MOLECULAR CHAPERONE HSP82 (chains A, B)
MASETFEFQAEITQLMSLIINTVYSNKEIFLREIVSNASDALDKIRYKSLSDPKQLETEP
DLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF
GVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD
QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIP

Ligands and cofactors

ID	Name	Formula	Copies
RDC	Radicicol	C18 H17 Cl O6	2

Primary citation

Structural Basis of the Radicicol Resistance Displayed by a Fungal Hsp90. Prodromou, C., Nuttall, J.M., Millson, S.H. et al. ACS Chem Biol (2009) 4:289. DOI 10.1021/CB9000316 · 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.
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
2YGE 1.96 Å, E88G-N92L Mutant of N-Term HSP90 complexed with Geldanamycin

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