1grh Summary



The structure was published by Karplus, P.A., Krauth-Siegel, R.L., Schirmer, R.H., and Schulz, G.E., in 1988 in a paper entitled "Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 1992.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of GLUTATHIONE REDUCTASE. This molecule has the UniProt identifier P00390 (GSHR_HUMAN)search. The sample contained 478 residues which is 92% of the natural sequence. Out of 478 residues 461 were observed and are deposited in the PDB.

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 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 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00390) Proteins of incorrect, partial and unknown sequencesearch FAD/NAD(P)-binding domainsearch, Enolase-like; domain 1search PF02852: Pyridine nucleotide-disulphide oxidoreductase, dimerisation domainsearch, PF07992: Pyridine nucleotide-disulphide oxidoreductasesearch

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

Chain InterPro annotation
A 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