6ATR
Crystal structure of hGSTA1-1 complexed with two GSH analogues in each subunit
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0004602 | molecular_function | glutathione peroxidase activity |
| A | 0004769 | molecular_function | steroid delta-isomerase activity |
| A | 0005504 | molecular_function | fatty acid binding |
| 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 | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030855 | biological_process | epithelial cell differentiation |
| A | 0043651 | biological_process | linoleic acid metabolic process |
| A | 0070062 | cellular_component | extracellular exosome |
| 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 | 0004602 | molecular_function | glutathione peroxidase activity |
| B | 0004769 | molecular_function | steroid delta-isomerase activity |
| B | 0005504 | molecular_function | fatty acid binding |
| 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 | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030855 | biological_process | epithelial cell differentiation |
| B | 0043651 | biological_process | linoleic acid metabolic process |
| B | 0070062 | cellular_component | extracellular exosome |
| 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 | 15 |
| Details | binding site for residue BWS A 301 |
| Chain | Residue |
| A | ARG45 |
| A | HOH525 |
| A | HOH614 |
| A | HOH641 |
| A | HOH655 |
| B | ASP101 |
| B | ARG131 |
| A | GLN54 |
| A | VAL55 |
| A | GLN67 |
| A | THR68 |
| A | PHE220 |
| A | GSN302 |
| A | HOH479 |
| A | HOH494 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue GSN A 302 |
| Chain | Residue |
| A | TYR9 |
| A | ARG15 |
| A | ARG45 |
| A | GLN54 |
| A | VAL55 |
| A | GLN67 |
| A | THR68 |
| A | PHE220 |
| A | BWS301 |
| A | EDO304 |
| A | HOH407 |
| A | HOH413 |
| A | HOH479 |
| A | HOH494 |
| A | HOH525 |
| A | HOH614 |
| A | HOH641 |
| A | HOH655 |
| A | HOH726 |
| B | ASP101 |
| B | ARG131 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ILE106 |
| A | TYR166 |
| A | GLU169 |
| A | LEU170 |
| A | EDO311 |
| A | HOH495 |
| A | HOH511 |
| A | HOH582 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | MET208 |
| A | GSN302 |
| A | HOH413 |
| A | HOH726 |
| A | HOH795 |
| A | HOH831 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | GLY48 |
| A | LEU50 |
| A | MET51 |
| A | GLN53 |
| A | HOH411 |
| A | HOH496 |
| A | HOH561 |
| B | LYS138 |
| B | HOH405 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | MET63 |
| A | LYS64 |
| A | HOH411 |
| A | HOH457 |
| A | HOH473 |
| A | HOH515 |
| A | HOH545 |
| A | HOH576 |
| A | HOH664 |
| B | MET94 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | GLU29 |
| A | PHE30 |
| A | PRO203 |
| A | HOH417 |
| A | HOH437 |
| A | HOH588 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 308 |
| Chain | Residue |
| A | ILE96 |
| A | ARG155 |
| A | HOH401 |
| A | HOH418 |
| A | HOH420 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 309 |
| Chain | Residue |
| A | GLU3 |
| A | LYS4 |
| A | PRO5 |
| A | VAL28 |
| A | GLU29 |
| A | HOH414 |
| A | HOH536 |
| A | HOH752 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 310 |
| Chain | Residue |
| A | HOH427 |
| A | HOH509 |
| A | HOH540 |
| A | HOH556 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 311 |
| Chain | Residue |
| A | ARG13 |
| A | LEU107 |
| A | TYR166 |
| A | EDO303 |
| A | HOH449 |
| A | HOH546 |
| A | HOH577 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | ARG13 |
| B | LEU107 |
| B | TYR166 |
| B | EDO304 |
| B | HOH411 |
| B | HOH536 |
| B | HOH551 |
| B | HOH583 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | ILE106 |
| B | TYR166 |
| B | GLU169 |
| B | LEU170 |
| B | EDO303 |
| B | HOH462 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | LEU72 |
| B | ILE96 |
| B | GLU97 |
| B | HIS159 |
| B | HOH459 |
| B | HOH627 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| B | GSN302 |
| B | HOH542 |
| B | HOH722 |
| B | HOH791 |
| B | HOH812 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 307 |
| Chain | Residue |
| B | ARG13 |
| B | TYR165 |
| B | GLU169 |
| B | ARG204 |
| B | HOH464 |
| B | HOH522 |
| B | HOH546 |
| B | HOH729 |
| site_id | AD8 |
| Number of Residues | 25 |
| Details | binding site for residues BWS B 301 and GSN B 302 |
| Chain | Residue |
| A | ASP101 |
| A | ARG131 |
| A | HOH403 |
| A | HOH548 |
| B | TYR9 |
| B | ARG15 |
| B | ARG45 |
| B | GLN54 |
| B | VAL55 |
| B | PRO56 |
| B | GLN67 |
| B | THR68 |
| B | PHE220 |
| B | EDO306 |
| B | HOH408 |
| B | HOH413 |
| B | HOH473 |
| B | HOH480 |
| B | HOH481 |
| B | HOH542 |
| B | HOH568 |
| B | HOH608 |
| B | HOH634 |
| B | HOH722 |
| B | HOH791 |
| site_id | AD9 |
| Number of Residues | 25 |
| Details | binding site for residues BWS B 301 and GSN B 302 |
| Chain | Residue |
| A | ASP101 |
| A | ARG131 |
| A | HOH403 |
| A | HOH548 |
| B | TYR9 |
| B | ARG15 |
| B | ARG45 |
| B | GLN54 |
| B | VAL55 |
| B | PRO56 |
| B | GLN67 |
| B | THR68 |
| B | PHE220 |
| B | EDO306 |
| B | HOH408 |
| B | HOH413 |
| B | HOH473 |
| B | HOH480 |
| B | HOH481 |
| B | HOH542 |
| B | HOH568 |
| B | HOH608 |
| B | HOH634 |
| B | HOH722 |
| B | HOH791 |
| site_id | AE1 |
| Number of Residues | 25 |
| Details | binding site for residues BWS B 301 and GSN B 302 |
| Chain | Residue |
| A | ASP101 |
| A | ARG131 |
| A | HOH403 |
| A | HOH548 |
| B | TYR9 |
| B | ARG15 |
| B | ARG45 |
| B | GLN54 |
| B | VAL55 |
| B | PRO56 |
| B | GLN67 |
| B | THR68 |
| B | PHE220 |
| B | EDO306 |
| B | HOH408 |
| B | HOH413 |
| B | HOH473 |
| B | HOH480 |
| B | HOH481 |
| B | HOH542 |
| B | HOH568 |
| B | HOH608 |
| B | HOH634 |
| B | HOH722 |
| B | HOH791 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965 |
| Chain | Residue | Details |
| A | TYR9 | |
| A | ARG45 | |
| A | GLN54 | |
| A | GLN67 | |
| B | TYR9 | |
| B | ARG45 | |
| B | GLN54 | |
| B | GLN67 |
| site_id | SWS_FT_FI2 |
| 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 | ALA2 | |
| B | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P30115 |
| Chain | Residue | Details |
| A | LYS4 | |
| B | LYS4 |
