human IFNw-IFNAR ternary complex. Determined by X-ray diffraction at 3.5 Å resolution. Released 31 Aug 2011.
Explore 3SE4 in 3D Show helices and sheets RCSB PDB PDBe
3SE4 contains 21 α-helices and 42 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 |
|---|---|---|---|
| β-strand | 11-14 | 4 | 1 |
| β-strand | 17-20 | 4 | 1 |
| β-strand | 33-40 | 8 | 2 |
| β-strand | 47-55 | 9 | 2 |
| α-helix | 59 | 1 | |
| β-strand | 60-61 | 2 | 1 |
| β-strand | 73-81 | 9 | 2 |
| β-strand | 84-89 | 6 | 2 |
| β-strand | 93 | 1 | 2 |
| α-helix | 95-98 | 4 | |
| β-strand | 105-110 | 6 | 3 |
| β-strand | 115-120 | 6 | 3 |
| α-helix | 130-133 | 4 | |
| β-strand | 137-144 | 8 | 4 |
| β-strand | 150-156 | 7 | 4 |
| β-strand | 159-162 | 4 | 3 |
| β-strand | 170-178 | 9 | 4 |
| β-strand | 185-188 | 4 | 4 |
| α-helix | 189-191 | 3 | |
| β-strand | 192-195 | 4 | 4 |
| α-helix | 196-197 | 2 | |
| α-helix | 203-205 | 3 | |
| β-strand | 206-213 | 8 | 5 |
| β-strand | 216-222 | 7 | 5 |
| β-strand | 229-236 | 8 | 6 |
| α-helix | 238-240 | 3 | |
| α-helix | 251 | 1 | |
| β-strand | 252 | 1 | 6 |
| α-helix | 253 | 1 | |
| β-strand | 259 | 1 | 6 |
| β-strand | 263-267 | 5 | 5 |
| α-helix | 268-270 | 3 | |
| β-strand | 275-283 | 9 | 6 |
| β-strand | 288-291 | 4 | 6 |
| α-helix | 292-294 | 3 | |
| β-strand | 295-298 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-22 | 13 | |
| α-helix | 28-31 | 4 | |
| α-helix | 52-70 | 19 | |
| α-helix | 75-77 | 3 | |
| α-helix | 81-98 | 18 | |
| α-helix | 118-136 | 19 | |
| α-helix | 140-157 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-19 | 9 | 7 |
| β-strand | 22-30 | 9 | 7 |
| β-strand | 38-45 | 8 | 8 |
| β-strand | 53-54 | 2 | 8 |
| β-strand | 61 | 1 | 8 |
| β-strand | 65-66 | 2 | 7 |
| β-strand | 78-86 | 9 | 8 |
| β-strand | 91-100 | 10 | 8 |
| α-helix | 101-104 | 4 | |
| β-strand | 106-107 | 2 | 7 |
| β-strand | 111-113 | 3 | 9 |
| β-strand | 116 | 1 | 9 |
| β-strand | 121-126 | 6 | 9 |
| β-strand | 140-146 | 7 | 10 |
| β-strand | 151-154 | 4 | 10 |
| β-strand | 165-170 | 6 | 9 |
| α-helix | 173-174 | 2 | |
| β-strand | 178-186 | 9 | 10 |
| α-helix | 194-198 | 5 | |
| β-strand | 199-202 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interferon alpha/beta receptor 1 | A | protein | 414 | Homo sapiens | P17181 (AlphaFold model) |
| Interferon omega-1 | B | protein | 177 | Homo sapiens | P05000 (AlphaFold model) |
| Interferon alpha/beta receptor 2 | C | protein | 199 | Homo sapiens | P48551 (AlphaFold model) |
>3SE4_1 Interferon alpha/beta receptor 1 (chains A) ADLGSKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNI TSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAI VIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKV KAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWL HAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEI KFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAER KIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSK
>3SE4_2 Interferon omega-1 (chains B) ADPLGCDLPQNHGLLSRNTLVLLHQMRRISPFLCLKDRRDFRFPQEMVKGSQLQKAHVMS VLHEMLQQIFSLFHTERSSAAWQMTLLDQLHTGLHQQLQHLETCLLQVVGEGESAGAISS PALTLRRYFQGIRVYLKEKKYSDCAWEVVRMEIMKSLFLSTNMQERLRSKDRDLGSS
>3SE4_3 Interferon alpha/beta receptor 2 (chains C) YTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFC DLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVK FPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLE HSDEQAVIKSPLKCTLLPP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Structural linkage between ligand discrimination and receptor activation by type I interferons. Thomas, C., Moraga, I., Levin, D. et al. Cell (2011) 146:621-632. DOI 10.1016/j.cell.2011.06.048 · PubMed
Other PDB entries of the same protein (UniProt P17181 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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