Human Glutathione Transferase O2 with glutathione -new crystal form
The structure was published by Zhou, H., Brock, J., Liu, D., Board, P.G., and Oakley, A.J., in 2012 in a paper entitled "Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Glutathione S-transferase omega-2. This molecule has the UniProt identifier Q9H4Y5 (GSTO2_HUMAN). The sample contained 239 residues which is 98% of the natural sequence. Out of 239 residues 238 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: