Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5. Determined by solution NMR. Released 3 Jun 2015.
Explore 2N0K in 3D Show helices and sheets RCSB PDB PDBe
2N0K contains 4 α-helices and 30 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 68-71 | 4 | 1 |
| β-strand | 74-77 | 4 | 1 |
| β-strand | 78-80 | 3 | 2 |
| β-strand | 90-93 | 4 | 3 |
| β-strand | 97-101 | 5 | 3 |
| β-strand | 103-108 | 6 | 4 |
| β-strand | 113-117 | 5 | 4 |
| β-strand | 120-123 | 4 | 3 |
| α-helix | 124-125 | 2 | |
| β-strand | 128 | 1 | 5 |
| α-helix | 130-132 | 3 | |
| β-strand | 134 | 1 | 6 |
| β-strand | 137 | 1 | 2 |
| β-strand | 142-144 | 3 | 2 |
| β-strand | 146 | 1 | 6 |
| β-strand | 147-148 | 2 | 1 |
| β-strand | 149 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-crystallin B chain | A, B | protein | 89 | Homo sapiens | P02511 (AlphaFold model) |
>2N0K_1 Alpha-crystallin B chain (chains A, B) GLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYR IPADVDPLTITSSLSSDGVLTVDGPRKQV
A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. Rajagopal, P., Tse, E., Borst, A.J. et al. Elife (2015) 4. DOI 10.7554/eLife.07304 · PubMed
Other PDB entries of the same protein (UniProt P02511 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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