Cryo-EM structure of human CNTFR alpha in complex with the Fab fragments of two antibodies. Determined by electron microscopy at 2.93 Å resolution. Released 29 Mar 2023.
Explore 8D7E in 3D Show helices and sheets RCSB PDB PDBe
8D7E contains 27 α-helices and 107 β-strands across 5 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 | 30-31 | 2 | |
| β-strand | 32-37 | 6 | 1 |
| β-strand | 42-44 | 3 | 2 |
| β-strand | 55-59 | 5 | 1 |
| β-strand | 62-63 | 2 | 1 |
| α-helix | 64-65 | 2 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 2 |
| β-strand | 73-76 | 4 | 2 |
| β-strand | 85-91 | 7 | 1 |
| β-strand | 97-106 | 10 | 1 |
| β-strand | 113-117 | 5 | 3 |
| β-strand | 118 | 1 | 4 |
| β-strand | 126-130 | 5 | 3 |
| β-strand | 140-147 | 8 | 5 |
| β-strand | 150-151 | 2 | 5 |
| α-helix | 175-176 | 2 | |
| β-strand | 177-184 | 8 | 5 |
| β-strand | 189-196 | 8 | 5 |
| β-strand | 202 | 1 | 4 |
| α-helix | 204-207 | 4 | |
| β-strand | 211-213 | 3 | 6 |
| β-strand | 223-225 | 3 | 6 |
| β-strand | 240-241 | 2 | 7 |
| β-strand | 243-248 | 6 | 8 |
| β-strand | 257-258 | 2 | 8 |
| β-strand | 264-266 | 3 | 6 |
| β-strand | 276-280 | 5 | 8 |
| β-strand | 283-284 | 2 | 7 |
| α-helix | 290-293 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 26 |
| β-strand | 18-25 | 8 | 26 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 27 |
| β-strand | 46-51 | 6 | 27 |
| β-strand | 58-60 | 3 | 27 |
| β-strand | 68-73 | 6 | 26 |
| β-strand | 78-83 | 6 | 26 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 27 |
| β-strand | 107-110 | 4 | 27 |
| β-strand | 114-116 | 3 | 27 |
| β-strand | 124 | 1 | 28 |
| β-strand | 127-131 | 5 | 29 |
| β-strand | 142-152 | 11 | 29 |
| β-strand | 153 | 1 | 28 |
| β-strand | 158-161 | 4 | 30 |
| α-helix | 162-164 | 3 | |
| β-strand | 170-172 | 3 | 29 |
| α-helix | 173-175 | 3 | |
| β-strand | 183-192 | 10 | 29 |
| α-helix | 193-195 | 3 | |
| β-strand | 201-207 | 7 | 30 |
| β-strand | 212-218 | 7 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 20 |
| β-strand | 10-13 | 4 | 21 |
| β-strand | 19-29 | 11 | 20 |
| β-strand | 33-38 | 6 | 21 |
| β-strand | 45-49 | 5 | 21 |
| β-strand | 53-54 | 2 | 21 |
| α-helix | 55 | 1 | |
| β-strand | 62-75 | 14 | 20 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 21 |
| α-helix | 96-97 | 2 | |
| β-strand | 99 | 1 | 21 |
| β-strand | 103-107 | 5 | 21 |
| β-strand | 112 | 1 | 22 |
| β-strand | 117-119 | 3 | 23 |
| α-helix | 123-126 | 4 | |
| β-strand | 130-140 | 11 | 23 |
| β-strand | 141 | 1 | 22 |
| β-strand | 146-150 | 5 | 24 |
| β-strand | 155 | 1 | 24 |
| β-strand | 160-164 | 5 | 23 |
| β-strand | 174-183 | 10 | 23 |
| α-helix | 184-189 | 6 | |
| β-strand | 192-193 | 2 | 25 |
| β-strand | 194-198 | 5 | 24 |
| β-strand | 207 | 1 | 24 |
| β-strand | 210-211 | 2 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 14 |
| β-strand | 11-12 | 2 | 15 |
| β-strand | 17-25 | 9 | 14 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 16 |
| β-strand | 45-51 | 7 | 16 |
| β-strand | 58-60 | 3 | 16 |
| β-strand | 68-73 | 6 | 14 |
| β-strand | 78-84 | 7 | 14 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-94 | 3 | 17 |
| β-strand | 95-97 | 3 | 16 |
| β-strand | 111-113 | 3 | 17 |
| β-strand | 114-115 | 2 | 15 |
| β-strand | 124-128 | 5 | 18 |
| β-strand | 139-149 | 11 | 18 |
| β-strand | 155-158 | 4 | 19 |
| α-helix | 159-161 | 3 | |
| β-strand | 163 | 1 | 19 |
| β-strand | 167-169 | 3 | 18 |
| α-helix | 170-172 | 3 | |
| β-strand | 173-174 | 2 | 18 |
| β-strand | 180-189 | 10 | 18 |
| α-helix | 190-193 | 4 | |
| β-strand | 199-204 | 6 | 19 |
| β-strand | 209-214 | 6 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 9 |
| β-strand | 10-13 | 4 | 10 |
| β-strand | 19-24 | 6 | 9 |
| α-helix | 28-29 | 2 | |
| α-helix | 30-32 | 3 | |
| β-strand | 34-39 | 6 | 10 |
| β-strand | 46-50 | 5 | 10 |
| β-strand | 54-55 | 2 | 10 |
| β-strand | 63-68 | 6 | 9 |
| β-strand | 71-76 | 6 | 9 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 10 |
| β-strand | 98-99 | 2 | 10 |
| β-strand | 103-107 | 5 | 10 |
| β-strand | 112 | 1 | 11 |
| β-strand | 115-119 | 5 | 12 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-128 | 6 | |
| β-strand | 130-140 | 11 | 12 |
| β-strand | 141 | 1 | 11 |
| β-strand | 146-150 | 5 | 13 |
| β-strand | 155 | 1 | 13 |
| β-strand | 160-164 | 5 | 12 |
| β-strand | 174-183 | 10 | 12 |
| α-helix | 184-187 | 4 | |
| β-strand | 192-198 | 7 | 13 |
| β-strand | 206-211 | 6 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ciliary neurotrophic factor receptor subunit alpha | C | protein | 348 | Homo sapiens | P26992 (AlphaFold model) |
| H4H25311P2 antibody Fab fragment light chain | G | protein | 215 | Homo sapiens | |
| H4H25311P2 antibody Fab fragment heavy chain | F | protein | 217 | Homo sapiens | |
| REGN8938 antibody Fab fragment light chain | E | protein | 215 | Homo sapiens | |
| REGN8938 antibody Fab fragment heavy chain | D | protein | 220 | Homo sapiens |
>8D7E_1 Ciliary neurotrophic factor receptor subunit alpha (chains C) QRHSPQEAPHVQYERLGSDVTLPCGTANWDAAVTWRVNGTDLAPDLLNGSQLVLHGLELG HSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFN VTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNATAITFDEFTIV KPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDG TAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAAETTTST TSSLAPPPTTKICDPGELGSEQKLISEEDLGGEQKLISEEDLHHHHHH
>8D7E_2 H4H25311P2 antibody Fab fragment light chain (chains G) EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGIP DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPWTFGQGTKVEIKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>8D7E_3 H4H25311P2 antibody Fab fragment heavy chain (chains F) QVQLVESGGGVVQPGRSLRLSCVASGFTFSTSVMHWVRQAPGKGLEWVANIWYDGINKFY VDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAREFWSAFDLWGQGTMVTVSSAST KGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY SLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVES
>8D7E_4 REGN8938 antibody Fab fragment light chain (chains E) DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPPITFGQGTRLEIKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>8D7E_5 REGN8938 antibody Fab fragment heavy chain (chains D) QVQLVESGGDVVQPGRSLRLSCAASGFTFSYYGMHWVRQPPGKGLEWVTIISFDGSQKYY ADSVKGRFTISRDNSKNTVFLQMNSLRTEDTGFYYCAAQSSTWPEYFQYWGQGTLVTVSS ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVES
Structural insights into the assembly of gp130 family cytokine signaling complexes. Zhou, Y., Stevis, P.E., Cao, J. et al. Sci Adv (2023) 9:eade4395-eade4395. DOI 10.1126/sciadv.ade4395 · PubMed
Other PDB entries of the same protein (UniProt P26992 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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