1AGS
A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030855 | biological_process | epithelial cell differentiation |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030855 | biological_process | epithelial cell differentiation |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GTX A 222 |
| Chain | Residue |
| A | GLN53 |
| A | GLN66 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GTX B 222 |
| Chain | Residue |
| B | GLN53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20083122 |
| Chain | Residue | Details |
| A | PHE9 | |
| A | ASN45 | |
| A | VAL54 | |
| A | THR67 | |
| B | PHE9 | |
| B | ASN45 | |
| B | VAL54 | |
| B | THR67 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P30115 |
| Chain | Residue | Details |
| A | GLU2 | |
| B | GLU2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P30115 |
| Chain | Residue | Details |
| A | PRO4 | |
| B | PRO4 |
