Structure analysis

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION

X-ray diffraction
1.7Å 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: 21388.88 Å2
Buried surface area: 8286.14 Å2
Dissociation area: 3,095.76 Å2
Dissociation energy (ΔGdiss): 46.09 kcal/mol
Dissociation entropy (TΔSdiss): 14.14 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-147405
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 21408.84 Å2
Buried surface area: 8128.72 Å2
Dissociation area: 3,018.32 Å2
Dissociation energy (ΔGdiss): 47.34 kcal/mol
Dissociation entropy (TΔSdiss): 14.13 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-147405

Macromolecules

Chains: A, B, C, D
Length: 273 amino acids
Theoretical weight: 30.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15559 (Residues: 2-274; Coverage: 100%)
Gene names: DIA4, NMOR1, NQO1
Pfam: Flavodoxin-like fold
InterPro:
CATH: Rossmann fold
SCOP: Quinone reductase

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