1CN4: Erythropoietin

Erythropoietin complexed with extracellular domains of erythropoietin receptor. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Aug 1999.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,604
Mol. weight: 69.01 kDa
Released: 11 Aug 1999

Explore 1CN4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CN4 contains 21 α-helices and 50 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: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	9-19	11
β-strand	27-29	3	1
β-strand	30	1	2
β-strand	37-42	6	1
β-strand	53-59	7	3
β-strand	65-67	3	3
α-helix	68	1
β-strand	70-73	4	1
β-strand	79-84	6	1
α-helix	87-89	3
β-strand	96-102	7	3
β-strand	106	1	3
β-strand	110-113	4	3
β-strand	119-120	2	2
α-helix	121-124	4
β-strand	125-128	4	4
β-strand	131	1	5
β-strand	138	1	5
β-strand	139-143	5	4
α-helix	151-153	3
β-strand	154-161	8	6
β-strand	169-174	6	6
β-strand	180-182	3	4
β-strand	191-200	10	6
β-strand	207-208	2	2
α-helix	209-215	7
β-strand	216-219	4	6

Chain B: 7 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	9-21	13
β-strand	27-29	3	7
β-strand	30	1	8
β-strand	37-42	6	7
β-strand	53-59	7	9
β-strand	65-67	3	9
β-strand	70	1	7
β-strand	73	1	7
β-strand	79-83	5	7
α-helix	87-89	3
β-strand	92	1	10
β-strand	96-102	7	9
β-strand	107-113	7	9
α-helix	115-117	3
β-strand	119	1	8
β-strand	125	1	11
β-strand	130-131	2	12
β-strand	138-141	4	12
β-strand	143	1	11
α-helix	144-145	2
α-helix	151-153	3
β-strand	154	1	13
β-strand	155-161	7	14
β-strand	171-176	6	14
β-strand	180-182	3	12
β-strand	191-195	5	14
β-strand	200	1	13
α-helix	201	1
β-strand	207	1	8
α-helix	209-215	7
β-strand	216-219	4	14

Chain C: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
α-helix	9-26	18
β-strand	34	1	15
β-strand	40-41	2	16
β-strand	46	1	10
α-helix	48-51	4
α-helix	56-82	27
α-helix	89-112	24
β-strand	133-134	2	16
β-strand	137	1	15
α-helix	138-148	11
α-helix	149-153	5
α-helix	154-160	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (erythropoietin receptor)	A, B	protein	228	Homo sapiens	P19235 (AlphaFold model)
Protein (erythropoietin)	C	protein	166	Homo sapiens	P01588 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1CN4_1 PROTEIN (ERYTHROPOIETIN RECEPTOR) (chains A, B)
REFAPPPNLPDPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSY
QLEDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINE
VVLLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEG
RTECVLSNLRGRTRYTFAVRARMAEPSFGGFWSEWSEPVSLLTPSDLD

Sequence of entity 2 (C), FASTA

>1CN4_2 PROTEIN (ERYTHROPOIETIN) (chains C)
APPRLICDSRVLERYLLEAKEAEKITTGCAEHCSLNEKITVPDTKVNFYAWKRMEVGQQA
VEVWQGLALLSEAVLRGQALLVKSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAIS
PPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR

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 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…
1ERN 2.4 Å, Native structure of the extracellular domain of erythropoietin (EPO) receptor [ebp]
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…
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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