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Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5

X-ray diffraction
1.7Å resolution
PDB entry 2gh5 coloured by chain, front view.
PDB entry 2gh5 coloured by chain, side view.
PDB entry 2gh5 coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Glutathione reductase, mitochondrial
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Multimeric state: homo dimer
Accessible surface area: 36996.69 Å2
Buried surface area: 14658.77 Å2
Dissociation area: 3,580.86 Å2
Dissociation energy (ΔGdiss): 53.3 kcal/mol
Dissociation entropy (TΔSdiss): 15.22 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-132462

Macromolecules

Glutathione reductase, mitochondrial
Chains: A, B
Length: 478 amino acids
Theoretical weight: 51.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00390 (Residues: 45-522; Coverage: 92%)
Gene names: GLUR, GRD1, GSR
Pfam:
InterPro:
CATH:
Glutathione reductase, mitochondrial in PDB entry 2gh5, assembly 1, front view.
Glutathione reductase, mitochondrial in PDB entry 2gh5, assembly 1, side view.
Glutathione reductase, mitochondrial in PDB entry 2gh5, assembly 1, top view.
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