2YGF: L89V, L93I and V136M Mutant of N-Term HSP90

L89V, L93I and V136M Mutant of N-Term HSP90 complexed with Geldanamycin. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Nov 2011.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 1
Atoms: 1,888
Mol. weight: 25.54 kDa
Ligands: GDM
Released: 16 Nov 2011

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

Secondary structure: helices and β-sheets

2YGF contains 14 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: 14 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	49-51	3
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	101-110	10
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	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	protein	220	SACCHAROMYCES CEREVISIAE	P02829 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2YGF_1 ATP-DEPENDENT MOLECULAR CHAPERONE HSP82 (chains A)
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEP
DLFIRITPKPEQKVLEIRDSGIGMTKAEVINNIGTIAKSGTKAFMEALSAGADVSMIGQF
GVGFYSLFLVADRVQMISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD
QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIP

Ligands and cofactors

ID	Name	Formula	Copies
GDM	Geldanamycin	C29 H40 N2 O9	1

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

Primary citation

Features of the Streptomyces Hygroscopicus Htpg Reveal How Partial Geldanamycin Resistance Can Arise by Mutation to the ATP Binding Pocket of a Eukaryotic Hsp90. Millson, S.H., Chua, C.S., Solovieva, S. et al. FASEB J (2011) 25:3828. DOI 10.1096/FJ.11-188821 · 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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