1AXD
STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000302 | biological_process | response to reactive oxygen species |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0009635 | biological_process | response to herbicide |
A | 0009751 | biological_process | response to salicylic acid |
A | 0016740 | molecular_function | transferase activity |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042542 | biological_process | response to hydrogen peroxide |
A | 0043295 | molecular_function | glutathione binding |
B | 0000302 | biological_process | response to reactive oxygen species |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0009635 | biological_process | response to herbicide |
B | 0009751 | biological_process | response to salicylic acid |
B | 0016740 | molecular_function | transferase activity |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042542 | biological_process | response to hydrogen peroxide |
B | 0043295 | molecular_function | glutathione binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR CHAIN C OF LACTOYLGLUTATHIONE |
Chain | Residue |
A | SER11 |
A | SER67 |
A | ARG68 |
A | HOH230 |
C | HOH6 |
C | HOH10 |
C | HOH57 |
A | ASN13 |
A | PHE35 |
A | HIS40 |
A | LYS41 |
A | GLN53 |
A | VAL54 |
A | PRO55 |
A | GLU66 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR CHAIN D OF LACTOYLGLUTATHIONE |
Chain | Residue |
B | SER11 |
B | ASN13 |
B | PHE35 |
B | HIS40 |
B | LYS41 |
B | GLN53 |
B | VAL54 |
B | PRO55 |
B | GLU66 |
B | SER67 |
B | HOH272 |
D | HOH145 |
D | HOH163 |
D | HOH237 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | TRP12 | |
B | TRP12 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS41 | |
A | VAL54 | |
A | SER67 | |
B | LYS41 | |
B | VAL54 | |
B | SER67 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
A | GLY7 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
B | GLY7 |