1XWK
2.3 angstrom resolution crystal structure of human glutathione S-transferase M1A-1A complexed with glutathionyl-S-dinitrobenzene
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018916 | biological_process | nitrobenzene metabolic process |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0042178 | biological_process | xenobiotic catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043295 | molecular_function | glutathione binding |
| A | 0051122 | biological_process | hepoxilin biosynthetic process |
| A | 0070458 | biological_process | cellular detoxification of nitrogen compound |
| A | 1901687 | biological_process | glutathione derivative biosynthetic process |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018916 | biological_process | nitrobenzene metabolic process |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0042178 | biological_process | xenobiotic catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043295 | molecular_function | glutathione binding |
| B | 0051122 | biological_process | hepoxilin biosynthetic process |
| B | 0070458 | biological_process | cellular detoxification of nitrogen compound |
| B | 1901687 | biological_process | glutathione derivative biosynthetic process |
| C | 0004364 | molecular_function | glutathione transferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006693 | biological_process | prostaglandin metabolic process |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0018916 | biological_process | nitrobenzene metabolic process |
| C | 0019899 | molecular_function | enzyme binding |
| C | 0042178 | biological_process | xenobiotic catabolic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0043295 | molecular_function | glutathione binding |
| C | 0051122 | biological_process | hepoxilin biosynthetic process |
| C | 0070458 | biological_process | cellular detoxification of nitrogen compound |
| C | 1901687 | biological_process | glutathione derivative biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDN A 218 |
| Chain | Residue |
| A | TRP7 |
| A | MET104 |
| A | HIS107 |
| A | MET108 |
| A | GLY111 |
| A | TYR115 |
| A | HOH224 |
| A | HOH236 |
| C | ASP105 |
| A | LEU12 |
| A | ARG42 |
| A | TRP45 |
| A | LYS49 |
| A | ASN58 |
| A | LEU59 |
| A | GLN71 |
| A | SER72 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDN B 219 |
| Chain | Residue |
| B | TRP7 |
| B | LEU12 |
| B | ARG42 |
| B | TRP45 |
| B | LYS49 |
| B | ASN58 |
| B | LEU59 |
| B | PRO60 |
| B | GLN71 |
| B | SER72 |
| B | MET104 |
| B | ASP105 |
| B | HIS107 |
| B | MET108 |
| B | GLY111 |
| B | TYR115 |
| B | HOH264 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDN C 220 |
| Chain | Residue |
| A | ASP105 |
| C | TRP7 |
| C | LEU12 |
| C | TRP45 |
| C | LYS49 |
| C | ASN58 |
| C | LEU59 |
| C | GLN71 |
| C | SER72 |
| C | MET104 |
| C | HIS107 |
| C | MET108 |
| C | GLY111 |
| C | TYR115 |
| C | HOH265 |
| C | HOH266 |
| C | HOH274 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 258 |
| Details | Domain: {"description":"GST N-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 354 |
| Details | Domain: {"description":"GST C-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2005","submissionDatabase":"PDB data bank","title":"Human glutathione S-transferase M1A-1A catalyzes formation of Gsh-metal complexes.","authors":["Patskovsky Y.V.","Patskovska L.N.","Listowsky I.","Almo S.C."]}},{"source":"PubMed","id":"16548513","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10649","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04905","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| A | TYR6 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| B | TYR6 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| C | TYR6 |
