2CZ3
Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from Mus musculus (form-2 crystal)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006559 | biological_process | L-phenylalanine catabolic process |
| A | 0006572 | biological_process | L-tyrosine catabolic process |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 1990748 | biological_process | cellular detoxification |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006559 | biological_process | L-phenylalanine catabolic process |
| B | 0006572 | biological_process | L-tyrosine catabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016034 | molecular_function | maleylacetoacetate isomerase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 1990748 | biological_process | cellular detoxification |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from Mus musculus (form-1 crystal).","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"}]} |
| 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 | SER10 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| B | SER10 |
