2gh5 Summary

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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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A glutathione reductase, mitochondrial P00390 (45-522) (GSHR_HUMAN)search Homo sapienssearch 92% 478 96%
B glutathione reductase, mitochondrial P00390 (45-522) (GSHR_HUMAN)search Homo sapienssearch 92% 478 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00390 (45 - 522) glutathione reductase, mitochondrial Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P00390) FAD/NAD(P)-binding domainsearch, Enolase-like; domain 1search PF02852: Pyridine nucleotide-disulphide oxidoreductase, dimerisation domainsearch, PF07992: Pyridine nucleotide-disulphide oxidoreductasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P00390) oxidation-reduction processsearch small molecule metabolic processsearch cell redox homeostasissearch glutathione metabolic processsearch nucleobase-containing small molecule interconversionsearch nucleobase-containing small molecule metabolic processsearch oxidoreductase activitysearch glutathione-disulfide reductase activitysearch electron carrier activitysearch flavin adenine dinucleotide bindingsearch NADP bindingsearch oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptorsearch mitochondrionsearch extracellular vesicular exosomesearch mitochondrial matrixsearch cytosolsearch external side of plasma membranesearch cytoplasmsearch

Chain InterPro annotation
A, B Pyridine nucleotide-disulphide oxidoreductase, NAD-binding domainsearch Pyridine nucleotide-disulphide oxidoreductase, dimerisation domainsearch Glutathione reductase, eukaryote/bacterialsearch Pyridine nucleotide-disulphide oxidoreductase, class I, active sitesearch FAD-dependent pyridine nucleotide-disulphide oxidoreductasesearch FAD/NAD-linked reductase, dimerisation domainsearch Pyridine nucleotide-disulphide oxidoreductase, FAD/NAD(P)-binding domainsearch