11QC: Human transferrin receptor ectodomain

Human transferrin receptor ectodomain. Determined by electron microscopy at 2.4 Å resolution. Released 27 May 2026.

Method: Electron microscopy
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 10,198
Mol. weight: 144.57 kDa
Ligands: NAG
Released: 27 May 2026

Explore 11QC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

11QC contains 69 α-helices and 62 β-strands across 2 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 A: 33 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	124-135	12
α-helix	140-146	7
β-strand	155	1	1
α-helix	160-175	16
β-strand	180-192	13	2
α-helix	197-198	2
β-strand	199-203	5	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
α-helix	264-273	10
β-strand	278-282	5	5
β-strand	297	1	6
β-strand	299-300	2	4
α-helix	317-319	3
β-strand	334-336	3	5
α-helix	339-346	8
β-strand	349	1	7
β-strand	352	1	8
α-helix	353-354	2
α-helix	355-357	3
α-helix	359-360	2
β-strand	364	1	8
β-strand	366	1	5
β-strand	367	1	7
β-strand	372-377	6	3
β-strand	380-393	14	2
β-strand	398-408	11	2
β-strand	411	1	1
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	471-474	4
β-strand	478-483	6	2
β-strand	488	1	2
β-strand	493-498	6	2
α-helix	500-502	3
α-helix	503-512	10
β-strand	514	1	9
α-helix	515	1
β-strand	521	1	9
α-helix	528-530	3
α-helix	532-535	4
α-helix	541-546	6
β-strand	552-558	7	2
α-helix	562-563	2
β-strand	568	1	6
α-helix	573-579	7
α-helix	583-603	21
α-helix	613-625	13
α-helix	626-628	3
α-helix	629-634	6
α-helix	640-662	23
α-helix	668-683	16
β-strand	686	1	10
β-strand	699	1	10
α-helix	709-716	8
α-helix	717-721	5
α-helix	728-750	23

Chain B: 36 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	124-135	12
α-helix	140-146	7
β-strand	155	1	11
α-helix	160-175	16
β-strand	180-192	13	12
α-helix	197-198	2
β-strand	199-203	5	13
β-strand	209-214	6	13
β-strand	220-221	2	14
β-strand	226-230	5	13
β-strand	232-234	3	15
α-helix	240-244	5
β-strand	254-258	5	15
α-helix	264-273	10
β-strand	278-282	5	15
β-strand	297	1	16
β-strand	299-300	2	14
α-helix	317-319	3
β-strand	334-336	3	15
α-helix	339-346	8
β-strand	349	1	17
β-strand	352	1	18
α-helix	353-354	2
α-helix	355-357	3
α-helix	359-360	2
β-strand	364	1	18
β-strand	366	1	15
β-strand	367	1	17
β-strand	372-377	6	13
β-strand	380-393	14	12
β-strand	398-408	11	12
β-strand	411	1	11
α-helix	416-420	5
α-helix	421-435	15
α-helix	436-440	5
β-strand	446-453	8	12
α-helix	456-458	3
α-helix	461-469	9
α-helix	471-474	4
β-strand	478-483	6	12
β-strand	488	1	12
β-strand	493-498	6	12
α-helix	500-502	3
α-helix	503-512	10
β-strand	514	1	19
α-helix	515	1
β-strand	521	1	19
α-helix	528-531	4
α-helix	532-535	4
α-helix	541-546	6
β-strand	552-558	7	12
α-helix	562-563	2
β-strand	568	1	16
α-helix	573-579	7
α-helix	583-603	21
α-helix	611-613	3
α-helix	614-625	12
α-helix	626-628	3
α-helix	629-634	6
α-helix	640-662	23
α-helix	668-679	12
α-helix	683-685	3
β-strand	686	1	20
β-strand	699	1	20
α-helix	709-716	8
α-helix	717-721	5
α-helix	728-750	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transferrin receptor protein 1, serum form	A, B	protein	639	Homo sapiens	P02786 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>11QC_1 Transferrin receptor protein 1, serum form (chains A, B)
LYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKV
WRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKK
DFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHA
HLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDS
TCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGV
GTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTY
INLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAA
FPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKL
THDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFG
NAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQ
NNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	6

Primary citation

Transferrin receptor 1 binds human parvovirus B19 VP1u to facilitate entry. Lee, H., Bieri, J., Ammann, N. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-74283-7 · PubMed

Other PDB entries of the same protein (UniProt P02786 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6OKD 1.85 Å, Crystal Structure of human transferrin receptor in complex with a cystine-dense peptide
8P0Z 1.88 Å, AP01-S2.3 - a variant of a redesigned transferrin receptor apical domain
6Y76 1.98 Å, AP01 - a redesigned transferrin receptor apical domain
9GH7 2.08 Å, Complex of human TfR1 with a potent bicyclic peptide
11RN 2.4 Å, Complex of B19V VP1u RBD and human transferrin receptor ectodomain
3KAS 2.4 Å, Machupo virus GP1 bound to human transferrin receptor 1
6WRV 2.47 Å, Crystal structure of computationally designed protein 3DS18 in complex with the human…
7ZQS 2.54 Å, Cryo-EM Structure of Human Transferrin Receptor 1 bound to DNA Aptamer
1DE4 2.8 Å, Hemochromatosis protein hfe complexed with transferrin receptor
6WRW 2.84 Å, Crystal structure of computationally designed protein 2DS25.5 in complex with the human…
6WRX 3.07 Å, Crystal structure of computationally designed protein 2DS25.1 in complex with the human…
1CX8 3.2 Å, Crystal structure of the ectodomain of human transferrin receptor

Browse structure collections

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