1EBA: Protein

Complex between the extracellular domain of erythropoietin (EPO) receptor [ebp] and an inactive peptide [EMP33] contains 3,5-dibromotyrosine in position 4 (denoted dby). Determined by X-ray diffraction at 2.7 Å resolution. Released 11 Nov 1998.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,536
Mol. weight: 51.99 kDa
Released: 11 Nov 1998

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

Secondary structure: helices and β-sheets

1EBA contains 19 α-helices and 40 β-strands across 4 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, 18 β-strands

Element	Residues	Length	Sheet
α-helix	11-18	8
β-strand	27-29	3	1
β-strand	30	1	2
β-strand	37-42	6	1
α-helix	50-52	3
β-strand	53-59	7	3
β-strand	62-67	6	3
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	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	144-145	2
α-helix	151-153	3
β-strand	154-162	9	5
β-strand	171-174	4	5
β-strand	180-183	4	4
α-helix	186-187	2
β-strand	191-200	10	5
α-helix	201	1
β-strand	207	1	2
α-helix	211-215	5
β-strand	216-219	4	5

Chain B: 9 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	11-18	8
β-strand	27-29	3	6
β-strand	30	1	7
β-strand	37-42	6	6
α-helix	50-52	3
β-strand	53-59	7	8
β-strand	65-66	2	8
β-strand	72-73	2	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	138-143	6	9
α-helix	144-145	2
α-helix	151-153	3
β-strand	154-162	9	10
β-strand	170-174	5	10
α-helix	175	1
β-strand	180-183	4	9
β-strand	191-200	10	10
β-strand	207	1	7
α-helix	212-215	4
β-strand	216-219	4	10

Chain C: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	11
β-strand	14-17	4	11

Chain D: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	11
β-strand	14-16	3	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (erythropoietin receptor)	A, B	protein	215	Homo sapiens	P19235 (AlphaFold model)
Protein (epo mimetics peptide 33)	C, D	protein	20

Sequence of entity 1 (A, B), FASTA

>1EBA_1 PROTEIN (ERYTHROPOIETIN RECEPTOR) (chains A, B)
KFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGNYSFSYQLEDEPWKLCRL
HQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVA
RLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVLSNLRGR
TRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDL

Sequence of entity 2 (C, D), FASTA

>1EBA_2 PROTEIN (EPO MIMETICS PEPTIDE 33) (chains C, D)
GGTYSCHFGPLTWVCKPQGG

Primary citation

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation. Livnah, O., Johnson, D.L., Stura, E.A. et al. Nat Struct Biol (1998) 5:993-1004. DOI 10.1038/2965 · 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
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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