6H5I: Ferritin heavy chain

Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex. Determined by electron microscopy at 3.9 Å resolution. Released 27 Mar 2019.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 26
Atoms: 43,900
Mol. weight: 626.41 kDa
Released: 27 Mar 2019

Explore 6H5I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6H5I contains 226 α-helices and 74 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.

Chain Aa: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-38	25
α-helix	49-75	27
β-strand	85	1	1
α-helix	97-123	27
α-helix	127-136	10
α-helix	138-158	21
α-helix	164-173	10

Chain Ab: 25 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	124-135	12
α-helix	141-147	7
α-helix	160-174	15
β-strand	180-193	14	2
β-strand	199-204	6	3
β-strand	210-214	5	3
β-strand	220-221	2	4
β-strand	227-230	4	3
β-strand	232-234	3	5
α-helix	240-243	4
β-strand	254-258	5	5
α-helix	264-273	10
β-strand	278-282	5	5
β-strand	299-300	2	4
β-strand	334-336	3	5
α-helix	340-346	7
β-strand	349-352	4	5
α-helix	353-354	2
β-strand	364-367	4	5
β-strand	371-376	6	3
β-strand	379-393	15	2
β-strand	398-408	11	2
α-helix	422-435	14
α-helix	436-440	5
β-strand	446-453	8	2
α-helix	461-468	8
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	6
β-strand	521	1	6
α-helix	532-535	4
α-helix	542-543	2
α-helix	544-548	5
β-strand	552-558	7	2
α-helix	562-563	2
α-helix	573-579	7
α-helix	583-603	21
α-helix	613-626	14
α-helix	629-633	5
α-helix	640-660	21
α-helix	671-679	9
α-helix	683-685	3
β-strand	686	1	7
β-strand	699	1	7
α-helix	709-717	9
α-helix	728-750	23

Chain Ac: 8 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-40	27
α-helix	49-76	28
β-strand	85	1	8
α-helix	86-88	3
α-helix	96-123	28
α-helix	127-136	10
α-helix	138-158	21
α-helix	164-169	6
α-helix	170-174	5

Chain Ad: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-38	25
α-helix	49-75	27
β-strand	85	1	9
α-helix	86-88	3
α-helix	97-123	27
α-helix	127-136	10
α-helix	138-157	20
α-helix	164-172	9

Chain Ae: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-38	25
α-helix	49-76	28
β-strand	85	1	1
α-helix	86-88	3
α-helix	96-122	27
α-helix	127-136	10
α-helix	138-158	21
α-helix	164-173	10

Chain Af: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-38	25
α-helix	49-75	27
β-strand	85	1	10
α-helix	86-88	3
α-helix	97-122	26
α-helix	127-136	10
α-helix	138-158	21
α-helix	164-174	11

Chain Ag: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-40	27
α-helix	49-75	27
β-strand	85	1	10
α-helix	86-88	3
α-helix	97-123	27
α-helix	127-136	10
α-helix	138-157	20
α-helix	164-173	10

Chain Ah: 8 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-38	25
α-helix	49-75	27
β-strand	85	1	8
α-helix	86-88	3
α-helix	97-123	27
α-helix	127-132	6
α-helix	133-137	5
α-helix	138-158	21
α-helix	164-173	10

17 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

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	172	Homo sapiens	P02794 (AlphaFold model)
Transferrin receptor protein 1	Ab, Aq	protein	640	Homo sapiens	P02786 (AlphaFold model)

Sequence of entity 1 (Aa, Ac, Ad, Ae, Af, Ag, Ah, Ai, Aj, Ak, Al, Am, An, Ao, Ap, Ar, As, At, Au, Av, Aw, Ax, Ay, Az), FASTA

>6H5I_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)
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEERE
HAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDK
NDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG

Sequence of entity 2 (Ab, Aq), FASTA

>6H5I_2 Transferrin receptor protein 1 (chains Ab, Aq)
RLYWDDLKRKLSEKLDSTDFTSTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSK
VWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTK
KDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGH
AHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTD
STCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSG
VGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFT
YINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNA
AFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIK
LTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDF
GNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRK
QNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF

Primary citation

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:

6B8F 1.06 Å, Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid
6B8G 1.13 Å, Twice-Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid
7A6A 1.15 Å, 1.15 A structure of human apoferritin obtained from Titan Mono- BCOR microscope
8B7O 1.17 Å, X-ray structure of Auranofin-human H-chain ferritin
6WYF 1.25 Å, Crystal structure of Human H-chain Ferritin variant 157C Delta C-star Modified with a…
6Z6U 1.25 Å, 1.25 A structure of human apoferritin obtained from Titan Mono-BCOR microscope
7RRP 1.27 Å, Apoferritin structure at 1.27 angstrom resolution determined from a 300 kV Titan Krios…
7A6B 1.33 Å, 1.33 A structure of human apoferritin obtained from Titan Mono- BCOR microscope
4Y08 1.34 Å, One minute iron loaded human H ferritin
7K3V 1.34 Å, Apoferritin structure at 1.34 angstrom resolution determined from a 300 kV Titan Krios…
7K3W 1.36 Å, Apoferritin structure at 1.36 angstrom resolution determined from a 300 kV Titan Krios…
9RGH 1.38 Å, X-ray structure of a polyoxidovanadate/human H-ferritin adduct obtained when the protein…

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