Structure analysis

X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values

X-ray diffraction
1.8Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 17300 Å2
Buried surface area: 8700 Å2
Dissociation area: 2,500 Å2
Dissociation energy (ΔGdiss): 27 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -23 kcal/mol
Symmetry number: 2

Macromolecules

Chains: A, B
Length: 231 amino acids
Theoretical weight: 25.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16083 (Residues: 1-231; Coverage: 100%)
Gene names: NMOR2, NQO2
Pfam: Flavodoxin-like fold
InterPro:
CATH: Rossmann fold

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