GLUTATHIONE TRANSFERASE FROM PROTEUS MIRABILIS
The structure was published by Rossjohn, J., Polekhina, G., Feil, S.C., et al., Masulli, M., De Illio, C., and Parker, M.W., in 1998 in a paper entitled "A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of GLUTATHIONE TRANSFERASE. This molecule has the UniProt identifier P15214 (GST_PROMI). The sample contained 203 residues which is 100% of the natural sequence. Out of 203 residues 201 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: