6Y76: Transferrin receptor protein 1

AP01 - a redesigned transferrin receptor apical domain. Determined by X-ray diffraction at 1.98 Å resolution. Released 22 Jul 2020.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,566
Mol. weight: 36.17 kDa
Released: 22 Jul 2020

Explore 6Y76 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Y76 contains 14 α-helices and 28 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: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	1
β-strand	14-19	6	1
β-strand	26	1	2
α-helix	28-30	3
β-strand	31-35	5	1
β-strand	37-39	3	3
α-helix	45-49	5
β-strand	59-63	5	3
β-strand	65	1	4
β-strand	67	1	4
α-helix	69-78	10
β-strand	83-87	5	3
α-helix	94-96	3
β-strand	99	1	2
β-strand	112-114	3	3
α-helix	117-125	9
β-strand	127-130	4	3
α-helix	131-132	2
α-helix	133-135	3
β-strand	142-145	4	3
β-strand	150-155	6	1

Chain B: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	5
β-strand	14-19	6	5
β-strand	26	1	6
α-helix	28-30	3
β-strand	31-35	5	5
β-strand	37-39	3	7
α-helix	45-50	6
β-strand	59-63	5	7
β-strand	65	1	8
β-strand	67	1	8
α-helix	69-78	10
β-strand	83-87	5	7
α-helix	94-96	3
β-strand	99	1	6
β-strand	112-114	3	7
α-helix	117-125	9
β-strand	127-130	4	7
α-helix	131-132	2
α-helix	133-135	3
β-strand	142-145	4	7
β-strand	150-155	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transferrin receptor protein 1	A, B	protein	168	Homo sapiens	P02786 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6Y76_1 Transferrin receptor protein 1 (chains A, B)
MQNSVIIVDKNGRLVYLVENPGGSVANSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIV
IVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFTGKGKSGIPVQTISRAAA
EKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSGSGSLEHHHHHH

Primary citation

Computational backbone design enables soluble engineering of transferrin receptor apical domain. Sjostrom, D.J., Berger, S.A., Oberdorfer, G. et al. Proteins (2020) 88:1569-1577. DOI 10.1002/prot.25974 · 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
9GH7 2.08 Å, Complex of human TfR1 with a potent bicyclic peptide
11QC 2.4 Å, Human transferrin receptor ectodomain
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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