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
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). 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):
This entry contains 1 unique UniProt protein: