CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE
The structure was published by Ji, X., Tordova, M., O'Donnell, R., et al., Hayden, J.B., Gilliland, G.L., and Zimniak, P., in 1997 in a paper entitled "Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1997.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of GLUTATHIONE S-TRANSFERASE.
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: