6ZB6
Crystal structure of Lolium rigidum GSTF in complex with S-(p-nitrobenzyl) glutathione
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0009635 | biological_process | response to herbicide |
| A | 0016740 | molecular_function | transferase activity |
| A | 0043295 | molecular_function | glutathione binding |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0009635 | biological_process | response to herbicide |
| B | 0016740 | molecular_function | transferase activity |
| B | 0043295 | molecular_function | glutathione binding |
| C | 0004364 | molecular_function | glutathione transferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0009635 | biological_process | response to herbicide |
| C | 0016740 | molecular_function | transferase activity |
| C | 0043295 | molecular_function | glutathione binding |
| D | 0004364 | molecular_function | glutathione transferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0009635 | biological_process | response to herbicide |
| D | 0016740 | molecular_function | transferase activity |
| D | 0043295 | molecular_function | glutathione binding |
| E | 0004364 | molecular_function | glutathione transferase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006749 | biological_process | glutathione metabolic process |
| E | 0009635 | biological_process | response to herbicide |
| E | 0016740 | molecular_function | transferase activity |
| E | 0043295 | molecular_function | glutathione binding |
| F | 0004364 | molecular_function | glutathione transferase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006749 | biological_process | glutathione metabolic process |
| F | 0009635 | biological_process | response to herbicide |
| F | 0016740 | molecular_function | transferase activity |
| F | 0043295 | molecular_function | glutathione binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue GTB A 301 |
| Chain | Residue |
| A | SER12 |
| A | TYR118 |
| A | PHE122 |
| A | MET126 |
| A | ARG127 |
| A | GOL302 |
| A | GOL303 |
| A | NA305 |
| A | HOH430 |
| A | HOH451 |
| A | HOH454 |
| A | THR13 |
| A | HOH499 |
| E | HIS107 |
| A | ASN14 |
| A | LYS42 |
| A | GLN54 |
| A | ILE55 |
| A | PRO56 |
| A | GLU67 |
| A | SER68 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | ASN14 |
| A | ARG69 |
| A | ASN110 |
| A | TYR175 |
| A | GTB301 |
| A | HOH451 |
| A | HOH453 |
| E | HIS107 |
| E | HOH452 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | MET11 |
| A | SER12 |
| A | PHE36 |
| A | GTB301 |
| A | HOH421 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | THR108 |
| A | HOH543 |
| E | GLN54 |
| E | HOH570 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | GTB301 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 306 |
| Chain | Residue |
| A | ASP85 |
| A | LEU86 |
| A | LEU87 |
| A | HOH409 |
| A | HOH488 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue GTB C 301 |
| Chain | Residue |
| C | SER12 |
| C | THR13 |
| C | ASN14 |
| C | HIS41 |
| C | LYS42 |
| C | GLN54 |
| C | ILE55 |
| C | PRO56 |
| C | GLU67 |
| C | SER68 |
| C | PHE122 |
| C | MET126 |
| C | TYR175 |
| C | GOL302 |
| C | HOH443 |
| C | HOH447 |
| C | HOH455 |
| C | HOH513 |
| F | HIS107 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| C | ASN14 |
| C | ARG69 |
| C | ASN110 |
| C | TYR175 |
| C | GTB301 |
| C | HOH434 |
| C | HOH447 |
| C | HOH461 |
| F | HIS107 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue NA C 303 |
| Chain | Residue |
| C | PRO3 |
| C | GLY61 |
| site_id | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue GTB E 301 |
| Chain | Residue |
| A | HIS107 |
| E | SER12 |
| E | THR13 |
| E | ASN14 |
| E | HIS41 |
| E | LYS42 |
| E | GLY53 |
| E | GLN54 |
| E | ILE55 |
| E | PRO56 |
| E | GLU67 |
| E | SER68 |
| E | VAL117 |
| E | PHE122 |
| E | TYR178 |
| E | GOL302 |
| E | HOH418 |
| E | HOH420 |
| E | HOH477 |
| E | HOH484 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL E 302 |
| Chain | Residue |
| E | TYR175 |
| E | GTB301 |
| E | HOH418 |
| E | HOH442 |
| E | HOH453 |
| A | HIS107 |
| E | ASN14 |
| E | ARG69 |
| E | ASN110 |
| site_id | AD3 |
| Number of Residues | 18 |
| Details | binding site for residue GTB B 301 |
| Chain | Residue |
| B | SER12 |
| B | THR13 |
| B | ASN14 |
| B | HIS41 |
| B | LYS42 |
| B | GLN54 |
| B | ILE55 |
| B | PRO56 |
| B | GLU67 |
| B | SER68 |
| B | VAL117 |
| B | TYR118 |
| B | PHE122 |
| B | TYR175 |
| B | GOL302 |
| B | HOH441 |
| B | HOH468 |
| B | HOH498 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | ASN14 |
| B | ARG69 |
| B | ASN110 |
| B | TYR175 |
| B | GTB301 |
| B | HOH441 |
| B | HOH447 |
| B | HOH454 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | MET11 |
| B | SER12 |
| B | PHE36 |
| B | HOH406 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | SER114 |
| B | PRO115 |
| B | TYR118 |
| B | GLN119 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| B | MET97 |
| B | TRP101 |
| B | ARG153 |
| B | HOH529 |
| B | HOH536 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 306 |
| Chain | Residue |
| B | GLU23 |
| B | ALA206 |
| B | HOH413 |
| B | HOH570 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 307 |
| Chain | Residue |
| B | PRO183 |
| F | GLY82 |
| F | HOH494 |
| site_id | AE1 |
| Number of Residues | 21 |
| Details | binding site for residue GTB F 301 |
| Chain | Residue |
| C | HIS107 |
| F | SER12 |
| F | THR13 |
| F | ASN14 |
| F | HIS41 |
| F | LYS42 |
| F | GLN54 |
| F | ILE55 |
| F | PRO56 |
| F | GLU67 |
| F | SER68 |
| F | TYR118 |
| F | PHE122 |
| F | TYR175 |
| F | GOL302 |
| F | HOH417 |
| F | HOH434 |
| F | HOH458 |
| F | HOH472 |
| F | HOH473 |
| F | HOH478 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL F 302 |
| Chain | Residue |
| C | HIS107 |
| F | ASN14 |
| F | ARG69 |
| F | ASN110 |
| F | GTB301 |
| F | HOH414 |
| F | HOH434 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue NA F 303 |
| Chain | Residue |
| B | HOH483 |
| B | HOH496 |
| F | ARG200 |
| F | HOH488 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue NA F 304 |
| Chain | Residue |
| B | HOH446 |
| B | HOH496 |
| F | HOH542 |
| site_id | AE5 |
| Number of Residues | 14 |
| Details | binding site for residue GSH D 301 |
| Chain | Residue |
| D | SER12 |
| D | ASN14 |
| D | LYS42 |
| D | GLN54 |
| D | ILE55 |
| D | PRO56 |
| D | GLU67 |
| D | SER68 |
| D | GOL302 |
| D | HOH417 |
| D | HOH419 |
| D | HOH449 |
| D | HOH461 |
| D | HOH542 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| D | ASN14 |
| D | ARG69 |
| D | ASN110 |
| D | TYR175 |
| D | GSH301 |
| D | HOH438 |
| D | HOH449 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue NA D 303 |
| Chain | Residue |
| D | ASP85 |
| D | ARG88 |
| D | GLY90 |
