NMR structure of the p62 PB1 domain. Determined by solution NMR. Released 15 Sept 2009.
Explore 2KKC in 3D Show helices and sheets RCSB PDB PDBe
2KKC contains 2 α-helices and 5 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 | 3-11 | 9 | 1 |
| β-strand | 17-26 | 10 | 1 |
| α-helix | 41-52 | 12 | |
| β-strand | 61-66 | 6 | 1 |
| β-strand | 72-75 | 4 | 1 |
| α-helix | 78-87 | 10 | |
| β-strand | 92-99 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sequestosome-1 | A | protein | 102 | Rattus norvegicus | O08623 (AlphaFold model) |
>2KKC_1 Sequestosome-1 (chains A) GPHMSLTVKAYLLGKEEAAREIRRFSFCFSPEPEAEAAAGPGPCERLLSRVAVLFPALRP GGFQAHYRAERGDLVAFSSDEELTMAMSYVKDDIFRIYIKEK
The NMR structure of the p62 PB1 domain, a key protein in autophagy and NF-kappaB signaling pathway. Saio, T., Yokochi, M., Inagaki, F. J Biomol NMR (2009) 45:335-341. DOI 10.1007/s10858-009-9370-7 · PubMed
Other PDB entries of the same protein (UniProt O08623 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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