3C11: ATP-dependent molecular chaperone HSP82

Yeast Hsp82 N-terminal domain-Geldanamycin complex: effects of mutants 98-99 KS-AA. Determined by X-ray diffraction at 1.6 Å resolution. Released 29 Jul 2008.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 2,175
Mol. weight: 27.72 kDa
Ligands: GDM
Released: 29 Jul 2008

Explore 3C11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3C11 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	4-7	4	1
α-helix	8-9	2
α-helix	10-21	12
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	101-110	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	240	Saccharomyces cerevisiae	P02829 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3C11_1 ATP-dependent molecular chaperone HSP82 (chains A)
MGSSHHHHHHSSGLVPRGSHMASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASD
ALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAAAG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTL
DEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIP

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

Crystal Structure of GRP94 with the Specific Mutation KS168-169AA with Bound Geldanamycin. Immormino, R.M., Metzger IV, L.E., Reardon, P.N. et al. To be published.

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
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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