Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5
The structure was published by Bauer, H., Fritz-Wolf, K., Winzer, A., et al., Palfey, B., Schirmer, R.H., and Davioud-Charvet, E., in 2006 in a paper entitled "A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2006.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of glutathione reductase, mitochondrial.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: