Retinoic acid receptor alpha mutant - N299H. Determined by X-ray diffraction at 1.9 Å resolution. Released 25 Jan 2023.
Explore 7WQQ in 3D Show helices and sheets RCSB PDB PDBe
7WQQ contains 15 α-helices and 5 β-strands across 2 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 | 182-198 | 17 | |
| α-helix | 202-204 | 3 | |
| β-strand | 208 | 1 | 1 |
| α-helix | 222-245 | 24 | |
| α-helix | 249-251 | 3 | |
| α-helix | 254-274 | 21 | |
| β-strand | 277-278 | 2 | 2 |
| β-strand | 283-285 | 3 | 2 |
| β-strand | 290 | 1 | 1 |
| β-strand | 291-293 | 3 | 2 |
| α-helix | 294-297 | 4 | |
| α-helix | 298-302 | 5 | |
| α-helix | 303-305 | 3 | |
| α-helix | 306-316 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 323-334 | 12 | |
| α-helix | 345-366 | 22 | |
| α-helix | 373-401 | 29 | |
| α-helix | 408-413 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 633-639 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoic acid receptor alpha | A | protein | 265 | Homo sapiens | P10276 (AlphaFold model) |
| Peptide from Nuclear receptor coactivator 1 | C | protein | 13 | Homo sapiens | Q15788 (AlphaFold model) |
>7WQQ_1 Retinoic acid receptor alpha (chains A) MKSSHHHHHHENLYFQSNAESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQ RVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTR YTPEQDTMTFSDGLTLNRTQMHHAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLIC GDRQDLEQPDRVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVI TLKMEIPGSMPPLIQEMLENSEGLD
>7WQQ_2 Peptide from Nuclear receptor coactivator 1 (chains C) RHKILHRLLQEGS
| ID | Name | Formula | Copies |
|---|---|---|---|
| 5Z6 | 4-[(E)-3-(3,5-ditert-butylphenyl)-3-oxidanylidene-prop-1-enyl]benzoic acid | C24 H28 O3 | 1 |
Effects of breast fibroepithelial tumor associated retinoic acid receptor alpha ligand binding domain mutations on receptor function and retinoid signaling. Huang, X.X., Ng, L.M., Teh, B.T. To be published.
Other PDB entries of the same protein (UniProt P10276 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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