human IFNa2-IFNAR ternary complex. Determined by X-ray diffraction at 4.0 Å resolution. Released 31 Aug 2011.
Explore 3SE3 in 3D Show helices and sheets RCSB PDB PDBe
3SE3 contains 25 α-helices and 47 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 | 11-12 | 2 | 1 |
| β-strand | 13-14 | 2 | 2 |
| β-strand | 19-20 | 2 | 1 |
| β-strand | 33-38 | 6 | 3 |
| β-strand | 47-48 | 2 | 3 |
| β-strand | 55 | 1 | 3 |
| β-strand | 59 | 1 | 1 |
| β-strand | 75-81 | 7 | 3 |
| β-strand | 84-90 | 7 | 3 |
| α-helix | 95-98 | 4 | |
| β-strand | 99-100 | 2 | 2 |
| α-helix | 101-104 | 4 | |
| β-strand | 105-110 | 6 | 4 |
| β-strand | 115-120 | 6 | 4 |
| α-helix | 130-135 | 6 | |
| β-strand | 137-144 | 8 | 5 |
| β-strand | 150-156 | 7 | 5 |
| β-strand | 159-162 | 4 | 4 |
| β-strand | 170-178 | 9 | 5 |
| β-strand | 185-188 | 4 | 5 |
| α-helix | 189-191 | 3 | |
| β-strand | 192-195 | 4 | 5 |
| α-helix | 199-200 | 2 | |
| α-helix | 203-205 | 3 | |
| β-strand | 209-213 | 5 | 6 |
| β-strand | 216-220 | 5 | 6 |
| β-strand | 229-230 | 2 | 7 |
| β-strand | 233-236 | 4 | 8 |
| α-helix | 237-241 | 5 | |
| α-helix | 250 | 1 | |
| β-strand | 251-252 | 2 | 8 |
| α-helix | 254-256 | 3 | |
| β-strand | 259 | 1 | 7 |
| β-strand | 263-266 | 4 | 6 |
| α-helix | 268-270 | 3 | |
| β-strand | 276-279 | 4 | 8 |
| β-strand | 281-283 | 3 | 7 |
| β-strand | 288-291 | 4 | 7 |
| α-helix | 292-294 | 3 | |
| β-strand | 295-297 | 3 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-20 | 12 | |
| α-helix | 27-32 | 6 | |
| α-helix | 40-42 | 3 | |
| α-helix | 53-66 | 14 | |
| α-helix | 70-75 | 6 | |
| α-helix | 78-97 | 20 | |
| α-helix | 115-132 | 18 | |
| α-helix | 137-155 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-18 | 7 | 9 |
| β-strand | 23-29 | 7 | 9 |
| β-strand | 38-45 | 8 | 10 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-54 | 2 | 10 |
| α-helix | 55 | 1 | |
| α-helix | 56-58 | 3 | |
| β-strand | 61 | 1 | 10 |
| β-strand | 65-67 | 3 | 9 |
| β-strand | 78-86 | 9 | 10 |
| β-strand | 91-100 | 10 | 10 |
| α-helix | 101-104 | 4 | |
| β-strand | 107 | 1 | 9 |
| α-helix | 108-110 | 3 | |
| β-strand | 111-116 | 6 | 11 |
| β-strand | 121-126 | 6 | 11 |
| β-strand | 140-147 | 8 | 12 |
| β-strand | 150-154 | 5 | 12 |
| β-strand | 166-170 | 5 | 11 |
| β-strand | 175 | 1 | 13 |
| β-strand | 179-186 | 8 | 12 |
| α-helix | 195-198 | 4 | |
| β-strand | 199-201 | 3 | 12 |
| β-strand | 203 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interferon alpha/beta receptor 1 | A | protein | 414 | Homo sapiens | P17181 (AlphaFold model) |
| Interferon alpha 2b | B | protein | 166 | Homo sapiens | P01563 (AlphaFold model) |
| Interferon alpha/beta receptor 2 | C | protein | 199 | Homo sapiens | P48551 (AlphaFold model) |
>3SE3_1 Interferon alpha/beta receptor 1 (chains A) ADLGSKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNI TSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAI VIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKV KAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWL HAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEI KFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAER KIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSK
>3SE3_2 Interferon alpha 2b (chains B) MCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLYNM ISQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
>3SE3_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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