mouse Interleukin-12 subunit beta - p80 homodimer in space group I41. Determined by X-ray diffraction at 2.4 Å resolution. Released 26 Aug 2020.
Explore 6SFF in 3D Show helices and sheets RCSB PDB PDBe
6SFF contains 5 α-helices and 28 β-strands across 1 chain. 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 | 24-27 | 4 | 1 |
| β-strand | 30-36 | 7 | 1 |
| β-strand | 44-49 | 6 | 2 |
| β-strand | 58-62 | 5 | 1 |
| β-strand | 70-71 | 2 | 1 |
| β-strand | 74-79 | 6 | 2 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-92 | 7 | 1 |
| β-strand | 95 | 1 | 1 |
| β-strand | 99-108 | 10 | 1 |
| β-strand | 111-112 | 2 | 1 |
| β-strand | 117 | 1 | 3 |
| β-strand | 127-129 | 3 | 3 |
| β-strand | 130 | 1 | 4 |
| β-strand | 136-143 | 8 | 3 |
| β-strand | 149-155 | 7 | 1 |
| β-strand | 165-167 | 3 | 3 |
| β-strand | 171-179 | 9 | 3 |
| β-strand | 182-193 | 12 | 3 |
| α-helix | 201-202 | 2 | |
| β-strand | 206-214 | 9 | 1 |
| β-strand | 217-225 | 9 | 1 |
| α-helix | 227-229 | 3 | |
| β-strand | 231 | 1 | 4 |
| α-helix | 233-236 | 4 | |
| β-strand | 237-244 | 8 | 5 |
| β-strand | 248-254 | 7 | 5 |
| β-strand | 268-274 | 7 | 6 |
| β-strand | 294-296 | 3 | 6 |
| β-strand | 300-303 | 4 | 5 |
| β-strand | 309-316 | 8 | 6 |
| α-helix | 322-326 | 5 | |
| β-strand | 327-330 | 4 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-12 subunit beta | A | protein | 344 | Mus musculus | P43432 (AlphaFold model) |
>6SFF_1 Interleukin-12 subunit beta (chains A) MCPQKLTISWFAIVLLVSPLMAMWELEKDVYVVEVDWTPDAPGETVNLTCDTPEEDDITW TSDQRHGVIGSGKTLTITVKEFLDAGQYTCHKGGETLSHSHLLLHKKENGIWSTEILKNF KNKTFLKCEAPNYSGRFTCSWLVQRNMDLKFNIKSSSSSPDSRAVTCGMASLSAEKVTLD QRDYEKYSVSCQEDVTCPTAEETLPIELALEARQQNKYENYSTSFFIRDIIKPDPPKNLQ MKPLKNSQVEVSWEYPDSWSTPHSYFSLKFFVRIQRKKEKMKETEEGCNQKGAFLVEKTS TEVQCKGGNVCVQAQDRYYNSSCSKWACVPCRVRSGTKHHHHHH
Homogeneously N-glycosylated proteins derived from the GlycoDelete HEK293 cell line enable diffraction-quality crystallogenesis. Kozak, S., Bloch, Y., De Munck, S. et al. Acta Crystallogr D Struct Biol (2020) 76:1244-1255. DOI 10.1107/S2059798320013753 · PubMed
Other PDB entries of the same protein (UniProt P43432 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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