Three-Dimensional NMR Structure of Rat Islet Amyloid Polypeptide in DPC micelles. Determined by solution NMR. Released 23 Jun 2009.
Explore 2KJ7 in 3D Show helices and sheets RCSB PDB PDBe
2KJ7 contains 2 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 20-23 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Islet amyloid polypeptide | A | protein | 38 | Rattus norvegicus | P12969 (AlphaFold model) |
>2KJ7_1 Islet amyloid polypeptide (chains A) KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYX
Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. Nanga, R.P., Brender, J.R., Xu, J. et al. J Am Chem Soc (2009) 131:8252-8261. DOI 10.1021/ja9010095 · PubMed
Other PDB entries of the same protein (UniProt P12969 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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