Solution Structure of Hepcidin-20. Determined by solution NMR. Released 6 Nov 2002.
Explore 1M4E in 3D Show helices and sheets RCSB PDB PDBe
1M4E 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 | 3-6 | 4 | 1 |
| β-strand | 14-17 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hepcidin | A | protein | 20 | P81172 (AlphaFold model) |
>1M4E_1 Hepcidin (chains A) ICIFCCGCCHRSKCGMCCKT
The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. Hunter, H.N., Fulton, D.B., Ganz, T. et al. J Biol Chem (2002) 277:37597-37603. DOI 10.1074/jbc.M205305200 · 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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