Solution NMR structures of human hepcidin at 325K. Determined by solution NMR. Released 23 Jun 2009.
Explore 2KEF in 3D Show helices and sheets RCSB PDB PDBe
2KEF contains 0 α-helices and 2 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 | 7-10 | 4 | 1 |
| β-strand | 20-23 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hepcidin | A | protein | 25 | Homo sapiens | P81172 (AlphaFold model) |
>2KEF_1 Hepcidin (chains A) DTHFPICIFCCGCCHRSKCGMCCKT
Hepcidin revisited, disulfide connectivity, dynamics, and structure. Jordan, J.B., Poppe, L., Haniu, M. et al. J Biol Chem (2009) 284:24155-24167. DOI 10.1074/jbc.M109.017764 · PubMed
Other PDB entries of the same protein (UniProt P81172 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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