Structure of Interleukin-23. Determined by X-ray diffraction at 2.3 Å resolution. Released 19 Aug 2008.
Explore 3DUH in 3D Show helices and sheets RCSB PDB PDBe
3DUH contains 23 α-helices and 53 β-strands across 4 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 | 1-5 | 5 | 1 |
| β-strand | 8-14 | 7 | 1 |
| β-strand | 22-27 | 6 | 2 |
| β-strand | 37-40 | 4 | 1 |
| β-strand | 48-49 | 2 | 1 |
| β-strand | 52-57 | 6 | 2 |
| α-helix | 60-62 | 3 | |
| β-strand | 64-70 | 7 | 1 |
| β-strand | 73-85 | 13 | 1 |
| β-strand | 90 | 1 | 1 |
| α-helix | 96-97 | 2 | |
| β-strand | 108-110 | 3 | 3 |
| β-strand | 111 | 1 | 4 |
| β-strand | 117-124 | 8 | 3 |
| β-strand | 130-138 | 9 | 1 |
| β-strand | 144-145 | 2 | 1 |
| β-strand | 146-148 | 3 | 3 |
| β-strand | 152-155 | 4 | 3 |
| β-strand | 165-173 | 9 | 3 |
| β-strand | 186-194 | 9 | 1 |
| β-strand | 197-205 | 9 | 1 |
| α-helix | 207-210 | 4 | |
| β-strand | 211 | 1 | 4 |
| α-helix | 213-216 | 4 | |
| β-strand | 217-223 | 7 | 5 |
| α-helix | 224 | 1 | |
| β-strand | 229-235 | 7 | 5 |
| β-strand | 249-257 | 9 | 6 |
| β-strand | 264-269 | 6 | 6 |
| β-strand | 273-277 | 5 | 5 |
| β-strand | 282-290 | 9 | 6 |
| α-helix | 296-300 | 5 | |
| β-strand | 301-304 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-5 | 5 | 7 |
| β-strand | 8-14 | 7 | 7 |
| β-strand | 22-27 | 6 | 8 |
| β-strand | 36-39 | 4 | 7 |
| β-strand | 48-49 | 2 | 7 |
| β-strand | 52-57 | 6 | 8 |
| α-helix | 60-62 | 3 | |
| β-strand | 64-70 | 7 | 7 |
| β-strand | 73-86 | 14 | 7 |
| β-strand | 89-90 | 2 | 7 |
| β-strand | 108-110 | 3 | 7 |
| β-strand | 111 | 1 | 9 |
| β-strand | 117-124 | 8 | 7 |
| β-strand | 130-138 | 9 | 7 |
| α-helix | 143 | 1 | |
| β-strand | 144-148 | 5 | 7 |
| β-strand | 152-155 | 4 | 7 |
| β-strand | 165-173 | 9 | 7 |
| α-helix | 185 | 1 | |
| β-strand | 186-194 | 9 | 7 |
| β-strand | 197-205 | 9 | 7 |
| α-helix | 207-210 | 4 | |
| β-strand | 211 | 1 | 9 |
| α-helix | 213-216 | 4 | |
| β-strand | 217-223 | 7 | 10 |
| β-strand | 230-235 | 6 | 10 |
| β-strand | 249-256 | 8 | 11 |
| β-strand | 265-269 | 5 | 11 |
| β-strand | 273-276 | 4 | 10 |
| β-strand | 283-290 | 8 | 11 |
| β-strand | 301-304 | 4 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| α-helix | 11-25 | 15 | |
| α-helix | 54-56 | 3 | |
| α-helix | 60-65 | 6 | |
| α-helix | 67-86 | 20 | |
| α-helix | 102-116 | 15 | |
| α-helix | 139-167 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-26 | 16 | |
| α-helix | 54-56 | 3 | |
| α-helix | 60-86 | 27 | |
| α-helix | 102-116 | 15 | |
| α-helix | 143-167 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-12 subunit beta | A, B | protein | 314 | Homo sapiens | P29460 (AlphaFold model) |
| Interleukin-23 subunit alpha | C, D | protein | 177 | Homo sapiens | Q9NPF7 (AlphaFold model) |
>3DUH_1 Interleukin-12 subunit beta (chains A, B) LEIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVK EFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRF TCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACP AAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPD TWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWS EWASVPCSHHHHHH
>3DUH_2 Interleukin-23 subunit alpha (chains C, D) LRAVPGGSSPAWTQCQQLSQKLCTLAWSAHPLVGHMDLREEGDEETTNDVPHIQCGDGCD PQGLRDNSQFCLQRIHQGLIFYEKLLGSDIFTGEPSLLPDSPVGQLHASLLGLSQLLQPE GHHWETQQIPSLSPSQPWQRLLLRFKILRSLQAFVAVAARVFAHGAATLSPHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
The structure of interleukin-23 reveals the molecular basis of p40 subunit sharing with interleukin-12. Lupardus, P.J., Garcia, K.C. J Mol Biol (2008) 382:931-941. DOI 10.1016/j.jmb.2008.07.051 · PubMed
Other PDB entries of the same protein (UniProt P29460 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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