Monomeric DARPin E2 complex with EpoR. Determined by X-ray diffraction at 2.09 Å resolution. Released 5 Jun 2019.
Explore 6MOE in 3D Show helices and sheets RCSB PDB PDBe
6MOE contains 43 α-helices and 35 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-14 | 11 | |
| α-helix | 18-26 | 9 | |
| α-helix | 41-48 | 8 | |
| α-helix | 51-59 | 9 | |
| α-helix | 74-81 | 8 | |
| α-helix | 84-92 | 9 | |
| α-helix | 107-113 | 7 | |
| α-helix | 117-125 | 9 | |
| α-helix | 140-146 | 7 | |
| α-helix | 150-161 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-15 | 12 | |
| α-helix | 18-26 | 9 | |
| α-helix | 41-48 | 8 | |
| α-helix | 51-59 | 9 | |
| α-helix | 74-81 | 8 | |
| α-helix | 84-92 | 9 | |
| α-helix | 107-113 | 7 | |
| α-helix | 117-125 | 9 | |
| α-helix | 140-146 | 7 | |
| α-helix | 150-161 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-21 | 14 | |
| β-strand | 27-29 | 3 | 1 |
| β-strand | 30 | 1 | 2 |
| β-strand | 36-42 | 7 | 1 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-59 | 7 | 3 |
| α-helix | 63-64 | 2 | |
| β-strand | 65-67 | 3 | 3 |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 79-85 | 7 | 1 |
| 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 | 154-161 | 8 | 5 |
| β-strand | 170-174 | 5 | 5 |
| α-helix | 175 | 1 | |
| 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 | 209-215 | 7 | |
| β-strand | 216-219 | 4 | 5 |
| α-helix | 220-222 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-21 | 13 | |
| β-strand | 27-29 | 3 | 6 |
| β-strand | 30 | 1 | 7 |
| β-strand | 35-42 | 8 | 6 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-59 | 7 | 8 |
| α-helix | 63-64 | 2 | |
| β-strand | 65-67 | 3 | 8 |
| β-strand | 70-73 | 4 | 6 |
| β-strand | 79-86 | 8 | 6 |
| α-helix | 91 | 1 | |
| β-strand | 95-102 | 8 | 8 |
| β-strand | 107-114 | 8 | 8 |
| 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 | 1 | |
| α-helix | 151-153 | 3 | |
| β-strand | 154-161 | 8 | 10 |
| β-strand | 168-174 | 7 | 10 |
| α-helix | 175 | 1 | |
| β-strand | 180-183 | 4 | 9 |
| α-helix | 186-187 | 2 | |
| β-strand | 191-200 | 10 | 10 |
| α-helix | 211-215 | 5 | |
| β-strand | 216-219 | 4 | 10 |
| α-helix | 220-222 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E2 DARPin | A, B | protein | 168 | synthetic construct | |
| Erythropoietin receptor | C, D | protein | 229 | Homo sapiens | P19235 (AlphaFold model) |
>6MOE_1 E2 DARPin (chains A, B) MGSDLGKKLLKAARAGQDDEVRILMANGADVNATDIWDATPLHLAALIGHLEIVEVLLKN GADVNASDITGTTPLHLAATMGHLEIVEVLLKYGADVNAYDLNGATPLHLAARMGHVEIV EVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQAAALEHHHHHH
>6MOE_2 Erythropoietin receptor (chains C, D) FAGSADPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSYQLEDE PWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLD APVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEGRTECV LSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDKEKAAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 9 |
Water and common crystallization additives (EPE, EDO) are not listed.
Topological control of cytokine receptor signaling induces differential effects in hematopoiesis. Mohan, K., Ueda, G., Kim, A.R. et al. Science (2019) 364. DOI 10.1126/science.aav7532 · 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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