2AKP: Hsp90 Delta24-N210 mutant

Hsp90 Delta24-N210 mutant. Determined by X-ray diffraction at 1.94 Å resolution. Released 31 Jan 2006.

Method: X-ray diffraction
Resolution: 1.94 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 3,145
Mol. weight: 41.92 kDa
Released: 31 Jan 2006

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

Secondary structure: helices and β-sheets

2AKP contains 21 α-helices and 14 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: 9 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	28-51	24
α-helix	54-57	4
β-strand	64-69	6	1
β-strand	74-79	6	1
α-helix	86-88	3
α-helix	89-93	5
α-helix	94-99	6
α-helix	102-108	7
α-helix	123-129	7
β-strand	131-139	9	1
β-strand	146-151	6	1
β-strand	157-160	4	1
β-strand	170-177	8	1
α-helix	179-185	7
α-helix	187-197	11
β-strand	205-207	3	1

Chain B: 12 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	30-49	20
α-helix	53-55	3
β-strand	64-69	6	2
α-helix	70-72	3
β-strand	74-79	6	2
α-helix	86-88	3
α-helix	89-93	5
α-helix	94-99	6
α-helix	102-110	9
α-helix	123-129	7
β-strand	131-139	9	2
β-strand	146-150	5	2
β-strand	157-160	4	2
α-helix	165-166	2
β-strand	170-177	8	2
α-helix	182-185	4
α-helix	187-197	11
α-helix	198-200	3
β-strand	205-207	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent molecular chaperone HSP82	A, B	protein	186	Saccharomyces cerevisiae	P02829 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2AKP_1 ATP-dependent molecular chaperone HSP82 (chains A, B)
SNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGM
TKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDE
QYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYP
IQLVVT

Primary citation

Intrinsic inhibition of the Hsp90 ATPase activity. Richter, K., Moser, S., Hagn, F. et al. J Biol Chem (2006) 281:11301-11311. DOI 10.1074/jbc.M510142200 · 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
2YGE 1.96 Å, E88G-N92L Mutant of N-Term HSP90 complexed with Geldanamycin

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