Solid-state NMR structure of the alpha-crystallin domain in alphaB-crystallin oligomers. Determined by solid-state NMR. Released 7 Jul 2010.
Explore 2KLR in 3D Show helices and sheets RCSB PDB PDBe
2KLR contains 2 α-helices and 12 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 | 74-79 | 6 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-94 | 6 | 2 |
| β-strand | 97-109 | 13 | 2 |
| β-strand | 112-123 | 12 | 2 |
| β-strand | 134-137 | 4 | 1 |
| β-strand | 143-148 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-crystallin B chain | A, B | protein | 175 | Homo sapiens | P02511 (AlphaFold model) |
>2KLR_1 Alpha-crystallin B chain (chains A, B) MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSW FDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHR KYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Jehle, S., Rajagopal, P., Bardiaux, B. et al. Nat Struct Mol Biol (2010) 17:1037-1042. DOI 10.1038/nsmb.1891 · 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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