1ERN: Protein

Native structure of the extracellular domain of erythropoietin (EPO) receptor [ebp]. Determined by X-ray diffraction at 2.4 Å resolution. Released 7 Jan 2000.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,337
Mol. weight: 47.02 kDa
Released: 7 Jan 2000

Explore 1ERN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ERN contains 18 α-helices and 37 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: 8 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	12-18	7
β-strand	27-29	3	1
β-strand	30	1	2
β-strand	37-43	7	1
α-helix	50-52	3
β-strand	53-58	6	3
β-strand	65-66	2	3
β-strand	70-72	3	1
β-strand	78-84	7	1
α-helix	87-89	3
β-strand	96-102	7	3
β-strand	107-113	7	3
α-helix	115-117	3
β-strand	119	1	2
α-helix	121-124	4
β-strand	125-131	7	4
β-strand	138-143	6	4
α-helix	144	1
α-helix	151-153	3
β-strand	154-162	9	5
β-strand	168-174	7	5
β-strand	180-183	4	4
α-helix	186-187	2
β-strand	191-200	10	5
β-strand	207	1	2
β-strand	216-219	4	5

Chain B: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	11-19	9
β-strand	27-29	3	6
β-strand	30	1	7
β-strand	37-42	6	6
α-helix	50-52	3
β-strand	53-58	6	8
α-helix	62-64	3
β-strand	65-67	3	8
β-strand	70-73	4	6
β-strand	79-84	6	6
α-helix	87-89	3
β-strand	96-102	7	8
β-strand	107-113	7	8
α-helix	115-117	3
β-strand	119	1	7
α-helix	121-124	4
β-strand	125-131	7	9
β-strand	137-143	7	9
α-helix	144-145	2
α-helix	151-153	3
β-strand	154-162	9	10
β-strand	168-172	5	10
β-strand	176	1	10
β-strand	182-184	3	9
β-strand	191-200	10	10
β-strand	207	1	7
α-helix	211-215	5
β-strand	216-219	4	10
α-helix	220-221	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (erythropoietin receptor)	A, B	protein	213	Homo sapiens	P19235 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1ERN_1 PROTEIN (ERYTHROPOIETIN RECEPTOR) (chains A, B)
KFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGNYSFSYQLEDEPWKLCRL
HQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVA
RLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVLSNLRGR
TRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPS

Primary citation

Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Livnah, O., Stura, E.A., Middleton, S.A. et al. Science (1999) 283:987-990. DOI 10.1126/science.283.5404.987 · PubMed

Other PDB entries of the same protein (UniProt P19235 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1EER 1.9 Å, Crystal structure of human erythropoietin complexed to its receptor at 1.9 Å
6MOI 2.06 Å, Dimeric DARPin C_angle_R5 complex with EpoR
6MOE 2.09 Å, Monomeric DARPin E2 complex with EpoR
8VUI 2.1 Å, Structure of FabS1CE-EPR-1, an elbow-locked Fab, in complex with the erythropoeitin…
6MOJ 2.43 Å, Dimeric DARPin A_angle_R5 complex with EpoR
4Y5V 2.6 Å, Diabody 305 complex with EpoR
6E2Q 2.65 Å, Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor
1EBA 2.7 Å, Complex between the extracellular domain of erythropoietin (EPO) receptor [ebp] and an…
1CN4 2.8 Å, Erythropoietin complexed with extracellular domains of erythropoietin receptor
1EBP 2.8 Å, Complex between the extracellular domain of erythropoietin (EPO) receptor [ebp] and an…
4Y5Y 2.85 Å, Diabody 330 complex with EpoR
6MOF 2.89 Å, Monomeric DARPin G2 complex with EpoR

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