Apoferritin structure at 1.27 angstrom resolution determined from a 300 kV Titan Krios G3i electron microscope with Falcon4 detector. Determined by electron microscopy at 1.27 Å resolution. Released 18 Aug 2021.
Explore 7RRP in 3D Show helices and sheets RCSB PDB PDBe
7RRP contains 192 α-helices and 24 β-strands across 24 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 |
|---|---|---|---|
| α-helix | 14-41 | 28 | |
| α-helix | 49-75 | 27 | |
| β-strand | 85 | 1 | 1 |
| α-helix | 86-88 | 3 | |
| α-helix | 96-123 | 28 | |
| α-helix | 127-133 | 7 | |
| α-helix | 134-138 | 5 | |
| α-helix | 139-158 | 20 | |
| α-helix | 164-173 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ferritin heavy chain | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | protein | 172 | Homo sapiens | P02794 (AlphaFold model) |
>7RRP_1 Ferritin heavy chain (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X) TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEERE HAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDK NDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 206 |
Water and common crystallization additives (NA) are not listed.
Resolving individual atoms of protein complex by cryo-electron microscopy. Zhang, K., Pintilie, G.D., Li, S. et al. Cell Res (2020) 30:1136-1139. DOI 10.1038/s41422-020-00432-2 · PubMed
Other PDB entries of the same protein (UniProt P02794 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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