Erythropoietin complexed with extracellular domains of erythropoietin receptor. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Aug 1999.
Explore 1CN4 in 3D Show helices and sheets RCSB PDB PDBe
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.
| 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 |
| 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 |
| 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 |
| 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) |
>1CN4_1 PROTEIN (ERYTHROPOIETIN RECEPTOR) (chains A, B) REFAPPPNLPDPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSY QLEDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINE VVLLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEG RTECVLSNLRGRTRYTFAVRARMAEPSFGGFWSEWSEPVSLLTPSDLD
>1CN4_2 PROTEIN (ERYTHROPOIETIN) (chains C) APPRLICDSRVLERYLLEAKEAEKITTGCAEHCSLNEKITVPDTKVNFYAWKRMEVGQQA VEVWQGLALLSEAVLRGQALLVKSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAIS PPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
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:
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