3VT7: Rat VDR-LBD with W282R mutation

Crystal structures of rat VDR-LBD with W282R mutation. Determined by X-ray diffraction at 1.65 Å resolution. Released 22 May 2013.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Rattus norvegicus
Chains
2
Atoms
2,141
Mol. weight
32.55 kDa
Ligands
VDX
Released
22 May 2013

Explore 3VT7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VT7 contains 15 α-helices and 0 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, 0 β-strands

ElementResiduesLengthSheet
α-helix126-14217
α-helix150-1523
α-helix154-1563
α-helix223-24220
α-helix247-2493
α-helix252-27019
α-helix271-2733
α-helix293-2975
α-helix303-31816
α-helix323-33412
α-helix345-36622
α-helix375-40228
α-helix404-4074
α-helix412-4187
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix628-6336

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vitamin D3 receptorAprotein271Rattus norvegicusP13053 (AlphaFold model)
Coactivator peptide dripCprotein13D3ZRN2
Sequence of entity 1 (A), FASTA
>3VT7_1 Vitamin D3 receptor (chains A)
GSHMGSPNSPLKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGS
VTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSN
QSFTMDDMSRDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLNLHEEEHVLLMAI
CIVSPDRPGVQDAKLVEAIQDRLSNTLQTYIRCRHPPPGSHQLYAKMIQKLADLRSLNEE
HSKQYRSLSFQPENSMKLTPLVLEVFGNEIS
Sequence of entity 2 (C), FASTA
>3VT7_2 COACTIVATOR PEPTIDE DRIP (chains C)
KNHPMLMNLLKDN

Ligands and cofactors

IDNameFormulaCopies
VDXCalcitriolC27 H44 O31

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:

Browse structure collections

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