Dimeric DARPin A_angle_R5 complex with EpoR. Determined by X-ray diffraction at 2.43 Å resolution. Released 5 Jun 2019.
Explore 6MOJ in 3D Show helices and sheets RCSB PDB PDBe
6MOJ contains 24 α-helices and 18 β-strands across 2 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 | 5-14 | 10 | |
| 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 | 107-114 | 8 | |
| α-helix | 117-125 | 9 | |
| α-helix | 140-146 | 7 | |
| α-helix | 150-157 | 8 | |
| α-helix | 173-179 | 7 | |
| α-helix | 183-190 | 8 | |
| α-helix | 206-213 | 8 | |
| α-helix | 216-224 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-21 | 13 | |
| 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 |
| α-helix | 63-64 | 2 | |
| β-strand | 65-67 | 3 | 3 |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 79-84 | 6 | 1 |
| β-strand | 96-102 | 7 | 3 |
| β-strand | 107-113 | 7 | 3 |
| α-helix | 115-117 | 3 | |
| β-strand | 119-120 | 2 | 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 |
| β-strand | 180-183 | 4 | 4 |
| α-helix | 186-187 | 2 | |
| β-strand | 191-200 | 10 | 5 |
| α-helix | 201 | 1 | |
| β-strand | 207-208 | 2 | 2 |
| α-helix | 209-215 | 7 | |
| β-strand | 216-219 | 4 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dimeric DARPin ACR5 (A_angle_R5) | A | protein | 231 | synthetic construct | |
| Erythropoietin receptor | B | protein | 229 | Homo sapiens | P19235 (AlphaFold model) |
>6MOJ_1 Dimeric DARPin ACR5 (A_angle_R5) (chains A) MGHHHHHHSDLGKKLLKAARAGQDDEVRILMANGADVNATDIWDATPLHLAALIGHLEIV EVLLKNGADVNASDITGTTPLHLAATMGHKDIVKVLLEYGADVNAYDLNGATPLHLAARM GHAKIVLLLLEQGADVNAQDAAGMTPLHLAAANGHAVIVALLLMHGADVNAKDAAGMTPL HLAAANGHEEIVILLLAMGADVNAQDKFGKTAFDISIDNGNEELAKVLQDH
>6MOJ_2 Erythropoietin receptor (chains B) FAGSADPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSYQLEDE PWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLD APVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEGRTECV LSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDKEKAAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| TAR | D(-)-tartaric acid | C4 H6 O6 | 3 |
Water and common crystallization additives (GOL) 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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