Structure analysis

Crystal structures of rat VDR-LBD with W282R mutation

X-ray diffraction
2.1Å resolution
Assemblies composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules


Assembly 1 (preferred)
Multimeric state: hetero dimer
Accessible surface area: 12000 Å2
Buried surface area: 2300 Å2
Dissociation area: 550 Å2
Dissociation energy (ΔGdiss): 4 kcal/mol
Dissociation entropy (TΔSdiss): 8 kcal/mol
Interface energy (ΔGint): -19 kcal/mol
Symmetry number: 1
Assembly 2
Multimeric state: monomeric
Accessible surface area: 11600 Å2
Buried surface area: 1200 Å2
Dissociation area: 600 Å2
Dissociation energy (ΔGdiss): 6 kcal/mol
Dissociation entropy (TΔSdiss): 5 kcal/mol
Interface energy (ΔGint): -8 kcal/mol
Symmetry number: 1


Chain: A
Length: 271 amino acids
Theoretical weight: 30.57 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
  • Canonical: P13053 (Residues: 116-423; Coverage: 62%)
Gene names: Nr1i1, Vdr
Pfam: Ligand-binding domain of nuclear hormone receptor
CATH: Retinoid X Receptor

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Chain: C
Length: 13 amino acids
Theoretical weight: 1.57 KDa
Source organism: Synthetic construct
Expression system: Not provided

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