3VT3: Rat VDR-LBD with R270L mutation

Crystal structures of rat VDR-LBD with R270L mutation. Determined by X-ray diffraction at 1.7 Å resolution. Released 22 May 2013.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Rattus norvegicus
Chains
2
Atoms
2,298
Mol. weight
32.69 kDa
Ligands
VDX
Released
22 May 2013

Explore 3VT3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 14 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix115-1195
α-helix126-14217
α-helix148-1525
α-helix154-1563
α-helix223-24220
α-helix247-2493
α-helix252-27120
β-strand275-27621
β-strand281-28331
β-strand290-29121
α-helix293-2975
α-helix303-31917
α-helix323-33412
α-helix345-36622
α-helix375-40228
α-helix404-4074
α-helix412-4187
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix628-6347

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vitamin D3 receptorAprotein271Rattus norvegicusP13053 (AlphaFold model)
Coactivator peptide dripCprotein13
Sequence of entity 1 (A), FASTA
>3VT3_1 Vitamin D3 receptor (chains A)
GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGS
VTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLLSN
QSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLNLHEEEHVLLMAI
CIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
Sequence of entity 2 (C), FASTA
>3VT3_2 COACTIVATOR PEPTIDE DRIP (chains C)
KNHPMLMNLLKDN

Ligands and cofactors

IDNameFormulaCopies
VDXCalcitriolC27 H44 O31

Water and common crystallization additives (FMT, EDO) are not listed.

Primary citation

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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