1ykc Summary

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human glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide

A publication describing this structure is not available. The depositing authors are Patskovsky, Y.V.search; Patskovska, L.N.search; Listowsky, I.search; Almo, S.C.search

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2005.

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 Mu 2.

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 S-transferase Mu 2 P28161 (2-218) (GSTM2_HUMAN)search Homo sapienssearch 100% 217 100%
B Glutathione S-transferase Mu 2 P28161 (2-218) (GSTM2_HUMAN)search Homo sapienssearch 100% 217 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P28161 (2 - 218) Glutathione S-transferase Mu 2 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P28161) Glutathione S-transferase (GST), C-terminal domainsearch, Glutathione S-transferase (GST), N-terminal domainsearch Glutaredoxinsearch, Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2search PF00043: Glutathione S-transferase, C-terminal domainsearch, PF02798: Glutathione S-transferase, N-terminal domainsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B (P28161) cytoplasmsearch extracellular vesicular exosomesearch sarcoplasmic reticulumsearch cytosolsearch receptor bindingsearch glutathione transferase activitysearch enzyme bindingsearch transferase activitysearch protein homodimerization activitysearch glutathione bindingsearch xenobiotic catabolic processsearch cellular detoxification of nitrogen compoundsearch positive regulation of ryanodine-sensitive calcium-release channel activitysearch glutathione derivative biosynthetic processsearch metabolic processsearch xenobiotic metabolic processsearch nitrobenzene metabolic processsearch glutathione metabolic processsearch relaxation of cardiac musclesearch negative regulation of ryanodine-sensitive calcium-release channel activitysearch regulation of skeletal muscle contraction by regulation of release of sequestered calcium ionsearch regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ionsearch cellular response to caffeinesearch small molecule metabolic processsearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch

Chain InterPro annotation
A, B Glutathione S-transferase, Mu classsearch Glutathione S-transferase, N-terminalsearch Glutathione S-transferase, C-terminalsearch Glutathione S-transferase, C-terminal-likesearch Thioredoxin-like foldsearch