Structure analysis

Structural and Biochemical Basis for the Binding Selectivity of PPARg to PGC-1a

X-ray diffraction
2.3Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 14039.81 Å2
Buried surface area: 2848.87 Å2
Dissociation area: 605.03 Å2
Dissociation energy (ΔGdiss): 6.22 kcal/mol
Dissociation entropy (TΔSdiss): 7.49 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-153377

Macromolecules

Chain: A
Length: 275 amino acids
Theoretical weight: 31.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37231 (Residues: 234-504; Coverage: 54%)
Gene names: NR1C3, PPARG
Pfam: Ligand-binding domain of nuclear hormone receptor
InterPro:
CATH: Retinoid X Receptor
SCOP: Nuclear receptor ligand-binding domain

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Chain: B
Length: 12 amino acids
Theoretical weight: 1.27 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UBK2 (Residues: 141-152; Coverage: 2%)
Gene names: LEM6, PGC1, PGC1A, PPARGC1, PPARGC1A

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