1F3A
CRYSTAL STRUCTURE OF MGSTA1-1 IN COMPLEX WITH GSH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0004601 | molecular_function | peroxidase activity |
A | 0004769 | molecular_function | steroid delta-isomerase activity |
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 | 0006805 | biological_process | xenobiotic metabolic process |
A | 0009617 | biological_process | response to bacterium |
A | 0016740 | molecular_function | transferase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0035634 | biological_process | response to stilbenoid |
A | 0035731 | molecular_function | dinitrosyl-iron complex binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043295 | molecular_function | glutathione binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
A | 1901687 | biological_process | glutathione derivative biosynthetic process |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0004769 | molecular_function | steroid delta-isomerase activity |
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 | 0006805 | biological_process | xenobiotic metabolic process |
B | 0009617 | biological_process | response to bacterium |
B | 0016740 | molecular_function | transferase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0035634 | biological_process | response to stilbenoid |
B | 0035731 | molecular_function | dinitrosyl-iron complex binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043295 | molecular_function | glutathione binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
B | 1901687 | biological_process | glutathione derivative biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GSH A 224 |
Chain | Residue |
A | TYR8 |
A | HOH498 |
A | HOH503 |
A | HOH611 |
A | HOH686 |
A | HOH754 |
B | ASP100 |
B | ARG130 |
B | HOH422 |
A | ARG14 |
A | LYS44 |
A | GLN53 |
A | VAL54 |
A | PRO55 |
A | GLN66 |
A | THR67 |
A | HOH382 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GSH B 226 |
Chain | Residue |
A | ASP100 |
A | ARG130 |
B | ARG14 |
B | LYS44 |
B | ASP52 |
B | GLN53 |
B | VAL54 |
B | PRO55 |
B | GLN66 |
B | THR67 |
B | HOH345 |
B | HOH464 |
B | HOH598 |
B | HOH636 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11027134 |
Chain | Residue | Details |
A | PHE9 | |
B | PHE9 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11027134 |
Chain | Residue | Details |
A | LYS45 | |
A | VAL54 | |
A | THR67 | |
B | LYS45 | |
B | VAL54 | |
B | THR67 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P80894 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115 |
Chain | Residue | Details |
A | GLY2 | |
B | GLY2 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P30115 |
Chain | Residue | Details |
A | PRO4 | |
B | PRO4 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
A | TYR8 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
B | TYR8 |