Crystal structures of rat VDR-LBD with R270L mutation. Determined by X-ray diffraction at 1.7 Å resolution. Released 22 May 2013.
Explore 3VT3 in 3D Show helices and sheets RCSB PDB PDBe
3VT3 contains 15 α-helices and 3 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 | 115-119 | 5 | |
| α-helix | 126-142 | 17 | |
| α-helix | 148-152 | 5 | |
| α-helix | 154-156 | 3 | |
| α-helix | 223-242 | 20 | |
| α-helix | 247-249 | 3 | |
| α-helix | 252-271 | 20 | |
| β-strand | 275-276 | 2 | 1 |
| β-strand | 281-283 | 3 | 1 |
| β-strand | 290-291 | 2 | 1 |
| α-helix | 293-297 | 5 | |
| α-helix | 303-319 | 17 | |
| α-helix | 323-334 | 12 | |
| α-helix | 345-366 | 22 | |
| α-helix | 375-402 | 28 | |
| α-helix | 404-407 | 4 | |
| α-helix | 412-418 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 628-634 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vitamin D3 receptor | A | protein | 271 | Rattus norvegicus | P13053 (AlphaFold model) |
| Coactivator peptide drip | C | protein | 13 |
>3VT3_1 Vitamin D3 receptor (chains A) GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGS VTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLLSN QSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLNLHEEEHVLLMAI CIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
>3VT3_2 COACTIVATOR PEPTIDE DRIP (chains C) KNHPMLMNLLKDN
| ID | Name | Formula | Copies |
|---|---|---|---|
| VDX | Calcitriol | C27 H44 O3 | 1 |
Water and common crystallization additives (FMT, EDO) are not listed.
Crystal structures of hereditary vitamin D-resistant rickets-associated vitamin D receptor mutants R270L and W282R bound to 1,25-dihydroxyvitamin D3 and synthetic ligands. Nakabayashi, M., Tsukahara, Y., Iwasaki-Miyamoto, Y. et al. J Med Chem (2013) 56:6745-6760. DOI 10.1021/jm400537h · PubMed
Other PDB entries of the same protein (UniProt P13053 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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