Monoextended DARPin M_R12 complex with EpoR. Determined by X-ray diffraction at 3.16 Å resolution. Released 5 Jun 2019.
Explore 6MOL in 3D Show helices and sheets RCSB PDB PDBe
6MOL contains 44 α-helices and 36 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 | 4-14 | 11 | |
| α-helix | 17-26 | 10 | |
| α-helix | 40-47 | 8 | |
| α-helix | 50-58 | 9 | |
| α-helix | 73-80 | 8 | |
| α-helix | 83-91 | 9 | |
| α-helix | 106-113 | 8 | |
| α-helix | 116-125 | 10 | |
| α-helix | 139-146 | 8 | |
| α-helix | 149-158 | 10 | |
| α-helix | 172-179 | 8 | |
| α-helix | 182-191 | 10 | |
| α-helix | 205-212 | 8 | |
| α-helix | 215-223 | 9 | |
| α-helix | 238-245 | 8 | |
| α-helix | 248-257 | 10 | |
| α-helix | 271-278 | 8 | |
| α-helix | 281-290 | 10 | |
| α-helix | 300-307 | 8 | |
| α-helix | 310-318 | 9 | |
| α-helix | 333-340 | 8 | |
| α-helix | 343-351 | 9 | |
| α-helix | 366-373 | 8 | |
| α-helix | 376-384 | 9 | |
| α-helix | 399-406 | 8 | |
| α-helix | 409-417 | 9 | |
| α-helix | 432-439 | 8 | |
| α-helix | 442-453 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-21 | 13 | |
| β-strand | 27-29 | 3 | 1 |
| β-strand | 30 | 1 | 2 |
| β-strand | 37-43 | 7 | 1 |
| β-strand | 53-58 | 6 | 3 |
| β-strand | 65-67 | 3 | 3 |
| β-strand | 70-74 | 5 | 1 |
| β-strand | 78-84 | 7 | 1 |
| β-strand | 95-102 | 8 | 3 |
| β-strand | 107-114 | 8 | 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 | 170-174 | 5 | 5 |
| α-helix | 175 | 1 | |
| β-strand | 180-183 | 4 | 4 |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-21 | 11 | |
| β-strand | 27-29 | 3 | 6 |
| β-strand | 30 | 1 | 7 |
| β-strand | 37-42 | 6 | 6 |
| β-strand | 53-58 | 6 | 8 |
| β-strand | 65-67 | 3 | 8 |
| β-strand | 70-74 | 5 | 6 |
| β-strand | 78-84 | 7 | 6 |
| β-strand | 95-102 | 8 | 8 |
| β-strand | 107-114 | 8 | 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 | 180-182 | 3 | 9 |
| β-strand | 191-200 | 10 | 10 |
| α-helix | 201 | 1 | |
| β-strand | 207 | 1 | 7 |
| α-helix | 209-215 | 7 | |
| β-strand | 216-219 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monoextended DARPin R12 (M_R12) | A | protein | 461 | synthetic construct | |
| Erythropoietin receptor | B, C | protein | 229 | Homo sapiens | P19235 (AlphaFold model) |
>6MOL_1 Monoextended DARPin R12 (M_R12) (chains A) MGSDLGKKLLKAARAGQDDEVRILMANGADVNATDIWDATPLHLAALIGHLEIVEVLLKN GADVNASDITGTTPLHLAATMGHLEIVEVLLKYGADVNAYDLNGATPLHLAARMGHVEIV EVLLKYGADVNAQDAAGGTPLHEAARAGHLEIVEVLLKYGADVNAVDAAGGTPLHEAARA GHLEIVEVLLKYGADVNAVDAAGGTPLHEAARAGHLEIVEVLLKYGADVNAVDAAGGTPL HEAARAGHLEIVEVLLKYGADVNAVDAAGGTPLHEAARAGHLEIVEVLLKYGADVNAVGT PLHKAARAGHLEIVEVLLKYGADVNATDIWDATPLHLAALIGHLEIVEVLLKNGADVNAS DITGTTPLHLAATMGHLEIVEVLLKYGADVNAYDLNGATPLHLAARMGHVEIVEVLLKYG ADVNAQDKFGKTAFDISIDNGNEDLAEILQAAALEHHHHHH
>6MOL_2 Erythropoietin receptor (chains B, C) FAGSADPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGQYSFSYQLEDE PWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLD APVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGQGAGSVQRVEILEGRTECV LSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDKEKAAA
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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