Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex at 5.5 Angstrom resolution. Determined by electron microscopy at 5.5 Å resolution. Released 27 Mar 2019.
Explore 6GSR in 3D Show helices and sheets RCSB PDB PDBe
6GSR contains 250 α-helices and 76 β-strands across 26 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 | 14-40 | 27 | |
| α-helix | 49-76 | 28 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 124-136 | 13 | |
| α-helix | 140-146 | 7 | |
| α-helix | 160-176 | 17 | |
| β-strand | 180-192 | 13 | 2 |
| α-helix | 197-198 | 2 | |
| β-strand | 199-204 | 6 | 3 |
| β-strand | 209-214 | 6 | 3 |
| β-strand | 220-221 | 2 | 4 |
| β-strand | 226-230 | 5 | 3 |
| β-strand | 232-234 | 3 | 5 |
| α-helix | 240-244 | 5 | |
| β-strand | 254-258 | 5 | 5 |
| β-strand | 260 | 1 | 6 |
| β-strand | 262 | 1 | 6 |
| α-helix | 264-272 | 9 | |
| β-strand | 278-282 | 5 | 5 |
| β-strand | 299-300 | 2 | 4 |
| β-strand | 334-336 | 3 | 5 |
| α-helix | 339-346 | 8 | |
| β-strand | 349-352 | 4 | 5 |
| α-helix | 353-354 | 2 | |
| α-helix | 355-357 | 3 | |
| β-strand | 364-367 | 4 | 5 |
| β-strand | 371-377 | 7 | 3 |
| β-strand | 380-393 | 14 | 2 |
| β-strand | 398-408 | 11 | 2 |
| α-helix | 416-420 | 5 | |
| α-helix | 421-438 | 18 | |
| β-strand | 446-453 | 8 | 2 |
| α-helix | 456-458 | 3 | |
| α-helix | 461-469 | 9 | |
| α-helix | 474-476 | 3 | |
| β-strand | 478-483 | 6 | 2 |
| β-strand | 488 | 1 | 2 |
| β-strand | 493-498 | 6 | 2 |
| α-helix | 500-502 | 3 | |
| α-helix | 503-510 | 8 | |
| β-strand | 514 | 1 | 7 |
| β-strand | 521 | 1 | 7 |
| α-helix | 528-531 | 4 | |
| α-helix | 532-535 | 4 | |
| α-helix | 541-542 | 2 | |
| α-helix | 543-548 | 6 | |
| β-strand | 552-558 | 7 | 2 |
| α-helix | 573-579 | 7 | |
| α-helix | 583-603 | 21 | |
| α-helix | 613-625 | 13 | |
| α-helix | 626-628 | 3 | |
| α-helix | 640-662 | 23 | |
| α-helix | 668-681 | 14 | |
| α-helix | 682-685 | 4 | |
| β-strand | 686 | 1 | 8 |
| β-strand | 699 | 1 | 8 |
| α-helix | 709-717 | 9 | |
| α-helix | 728-749 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ferritin heavy chain | Aa, Ac, Ad, Ae, Af, Ag, Ah, Ai, Aj, Ak, Al, Am, An, Ao, Ap, Ar, As, At, Au, Av, Aw, Ax, Ay, Az | protein | 182 | Homo sapiens | P02794 (AlphaFold model) |
| Transferrin receptor protein 1 | Ab, Aq | protein | 640 | Homo sapiens | P02786 (AlphaFold model) |
>6GSR_1 Ferritin heavy chain (chains Aa, Ac, Ad, Ae, Af, Ag, Ah, Ai, Aj, Ak, Al, Am, An, Ao, Ap, Ar, As, At, Au, Av, Aw, Ax, Ay, Az) TTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSH EEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKL ATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDN ES
>6GSR_2 Transferrin receptor protein 1 (chains Ab, Aq) RLYWDDLKRKLSEKLDSTDFTSTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSK VWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTK KDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGH AHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTD STCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSG VGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFT YINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNA AFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIK LTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDF GNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRK QNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF
Cryo-EM structure of the human ferritin-transferrin receptor 1 complex. Montemiglio, L.C., Testi, C., Ceci, P. et al. Nat Commun (2019) 10:1121-1121. DOI 10.1038/s41467-019-09098-w · 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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