Crystal structure of the middle domain of human HSP90-beta refined at 2.3 A resolution. Determined by X-ray diffraction at 2.28 Å resolution. Released 15 Dec 2010.
Explore 3PRY in 3D Show helices and sheets RCSB PDB PDBe
3PRY contains 39 α-helices and 38 β-strands across 3 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 288-290 | 3 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-309 | 12 | |
| β-strand | 317-323 | 7 | 1 |
| β-strand | 329-335 | 7 | 1 |
| β-strand | 353-357 | 5 | 1 |
| β-strand | 360-363 | 4 | 1 |
| α-helix | 367-369 | 3 | |
| α-helix | 372-374 | 3 | |
| β-strand | 378-383 | 6 | 1 |
| α-helix | 395-420 | 26 | |
| α-helix | 423-443 | 21 | |
| α-helix | 445-447 | 3 | |
| α-helix | 448-453 | 6 | |
| β-strand | 456-457 | 2 | 2 |
| β-strand | 458-459 | 2 | 3 |
| β-strand | 467-468 | 2 | 2 |
| α-helix | 469-474 | 6 | |
| β-strand | 482-486 | 5 | 3 |
| α-helix | 491-495 | 5 | |
| α-helix | 498-504 | 7 | |
| β-strand | 510-512 | 3 | 3 |
| α-helix | 518-525 | 8 | |
| β-strand | 527-528 | 2 | 3 |
| β-strand | 531-535 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 288-290 | 3 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-309 | 12 | |
| α-helix | 314-315 | 2 | |
| β-strand | 317-323 | 7 | 4 |
| β-strand | 329-335 | 7 | 4 |
| β-strand | 353-357 | 5 | 4 |
| β-strand | 360-363 | 4 | 4 |
| α-helix | 367-369 | 3 | |
| α-helix | 372-374 | 3 | |
| β-strand | 378-383 | 6 | 4 |
| α-helix | 399-419 | 21 | |
| α-helix | 423-443 | 21 | |
| α-helix | 448-452 | 5 | |
| β-strand | 457 | 1 | 5 |
| β-strand | 458-459 | 2 | 6 |
| β-strand | 467 | 1 | 5 |
| α-helix | 469-474 | 6 | |
| β-strand | 483-487 | 5 | 6 |
| α-helix | 491-495 | 5 | |
| α-helix | 498-505 | 8 | |
| β-strand | 510-513 | 4 | 6 |
| α-helix | 518-525 | 8 | |
| β-strand | 527-528 | 2 | 7 |
| β-strand | 531-532 | 2 | 7 |
| β-strand | 533-535 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 288-290 | 3 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-309 | 12 | |
| α-helix | 314-315 | 2 | |
| β-strand | 317-323 | 7 | 8 |
| β-strand | 329-335 | 7 | 8 |
| β-strand | 353-357 | 5 | 8 |
| β-strand | 361-363 | 3 | 8 |
| α-helix | 367-369 | 3 | |
| β-strand | 378-383 | 6 | 8 |
| α-helix | 394-419 | 26 | |
| α-helix | 423-443 | 21 | |
| α-helix | 445-447 | 3 | |
| α-helix | 448-454 | 7 | |
| β-strand | 456-457 | 2 | 9 |
| β-strand | 459 | 1 | 10 |
| β-strand | 467-468 | 2 | 9 |
| α-helix | 469-474 | 6 | |
| β-strand | 483-487 | 5 | 10 |
| α-helix | 491-495 | 5 | |
| α-helix | 498-505 | 8 | |
| β-strand | 510-513 | 4 | 10 |
| α-helix | 517-525 | 9 | |
| β-strand | 527-528 | 2 | 11 |
| β-strand | 531-532 | 2 | 11 |
| β-strand | 533-535 | 3 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heat shock protein HSP 90-beta | A, B, C | protein | 268 | Homo sapiens | P08238 (AlphaFold model) |
>3PRY_1 Heat shock protein HSP 90-beta (chains A, B, C) MKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFD LFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILK VIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQS GDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCV QQLKEFDGKSLVSVTKEGLELAENLYFQ
Crystal structure of the middle domain of human HSP90-beta refined at 2.3 A resolution. Chaikuad, A., Pilka, E., Sharpe, T.D. et al. To be published.
Other PDB entries of the same protein (UniProt P08238 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3PRY directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.