Structure analysis

Crystal structures of rat VDR-LBD with R270L mutation

X-ray diffraction
1.9Å resolution
Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 11800 Å2
Buried surface area: 2200 Å2
Dissociation area: 550 Å2
Dissociation energy (ΔGdiss): 4 kcal/mol
Dissociation entropy (TΔSdiss): 7 kcal/mol
Interface energy (ΔGint): -16 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 11400 Å2
Buried surface area: 1100 Å2
Dissociation area: 550 Å2
Dissociation energy (ΔGdiss): 5 kcal/mol
Dissociation entropy (TΔSdiss): 5 kcal/mol
Interface energy (ΔGint): -7 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 271 amino acids
Theoretical weight: 30.55 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13053 (Residues: 116-423; Coverage: 62%)
Gene names: Nr1i1, Vdr
Pfam: Ligand-binding domain of nuclear hormone receptor
InterPro:
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
UniProt:

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