1EER: Human erythropoietin complexed to its receptor

Crystal structure of human erythropoietin complexed to its receptor at 1.9 Å. Determined by X-ray diffraction at 1.9 Å resolution. Released 1 Oct 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,917
Mol. weight: 68.84 kDa
Released: 1 Oct 1999

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

Secondary structure: helices and β-sheets

1EER contains 28 α-helices and 40 β-strands across 3 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: 10 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
α-helix	9-25	17
α-helix	26-28	3
β-strand	34-41	8	1
β-strand	46	1	2
α-helix	48-51	4
α-helix	56-82	27
α-helix	91-111	21
α-helix	114-120	7
β-strand	133-137	5	1
α-helix	138-148	11
α-helix	149-153	5
α-helix	154-161	8

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	9-21	13
β-strand	27-29	3	3
β-strand	30	1	4
β-strand	37-42	6	3
β-strand	53-59	7	5
β-strand	65-67	3	5
β-strand	69-74	6	3
β-strand	78-84	7	3
α-helix	87-89	3
β-strand	92	1	2
β-strand	96-102	7	5
β-strand	107-113	7	5
α-helix	115-117	3
β-strand	119-120	2	4
α-helix	121-124	4
β-strand	125-131	7	6
β-strand	138-143	6	6
α-helix	144-145	2
α-helix	151-153	3
β-strand	154-161	8	7
β-strand	171-174	4	7
β-strand	180-183	4	6
β-strand	191-200	10	7
α-helix	201	1
β-strand	207-208	2	4
α-helix	211-215	5
β-strand	216-219	4	7

Chain C: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	9-21	13
β-strand	27-29	3	8
β-strand	30	1	9
β-strand	37-42	6	8
α-helix	50-52	3
β-strand	53-59	7	10
β-strand	65-66	2	10
β-strand	70-73	4	8
β-strand	79-84	6	8
α-helix	87-89	3
β-strand	96-102	7	10
β-strand	107-113	7	10
α-helix	115-117	3
β-strand	119	1	9
α-helix	121-124	4
β-strand	125-131	7	11
β-strand	138-143	6	11
α-helix	144	1
α-helix	151-153	3
β-strand	154-162	9	12
β-strand	171-174	4	12
β-strand	180-183	4	11
α-helix	186-187	2
β-strand	191-200	10	12
α-helix	201	1
β-strand	207	1	9
α-helix	211-215	5
β-strand	216-219	4	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Erythropoietin	A	protein	166	Homo sapiens	P01588 (AlphaFold model)
Erythropoietin receptor	B, C	protein	227	Homo sapiens	P19235 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1EER_1 ERYTHROPOIETIN (chains A)
APPRLICDSRVLERYLLEAKEAEKITTGCAEHCSLNEKITVPDTKVNFYAWKRMEVGQQA
VEVWQGLALLSEAVLRGQALLVKSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAIS
NSDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR

Sequence of entity 2 (B, C), FASTA

>1EER_2 ERYTHROPOIETIN RECEPTOR (chains B, C)
REFPPPNPDPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSYQL
EDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVV
LLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEGRT
ECVLSNLRGRTRYTFAVRARMAEPSFGGFWSEWSEPVSLLTPSDLDP

Primary citation

Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Syed, R.S., Reid, S.W., Li, C. et al. Nature (1998) 395:511-516. DOI 10.1038/26773 · PubMed

Other PDB entries of the same protein (UniProt P01588 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CN4 2.8 Å, Erythropoietin complexed with extracellular domains of erythropoietin receptor
1BUY Human erythropoietin, NMR minimized average structure

Browse more

1EER is part of these collections:

Insulin and hormones

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