Structure of the tetragonal form of the N-terminal domain of the yeast HSP90 chaperone. Determined by X-ray diffraction at 1.8 Å resolution. Released 22 Oct 1997.
Explore 1AH6 in 3D Show helices and sheets RCSB PDB PDBe
1AH6 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.
| 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 | 97-98 | 2 | |
| α-helix | 101-110 | 10 | |
| α-helix | 114-120 | 7 | |
| α-helix | 123-129 | 7 | |
| β-strand | 131-139 | 9 | 1 |
| β-strand | 145-150 | 6 | 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein 90 | A | protein | 220 | Saccharomyces cerevisiae | P02829 (AlphaFold model) |
>1AH6_1 HEAT SHOCK PROTEIN 90 (chains A) MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEP DLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF GVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIP
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Prodromou, C., Roe, S.M., Piper, P.W. et al. Nat Struct Biol (1997) 4:477-482. DOI 10.1038/nsb0697-477 · PubMed
Other PDB entries of the same protein (UniProt P02829 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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