1GUL
HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE
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 | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0004364 | molecular_function | glutathione transferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0006805 | biological_process | xenobiotic metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0004364 | molecular_function | glutathione transferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0006805 | biological_process | xenobiotic metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| E | 0004364 | molecular_function | glutathione transferase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0006749 | biological_process | glutathione metabolic process |
| E | 0006805 | biological_process | xenobiotic metabolic process |
| E | 0016740 | molecular_function | transferase activity |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0042803 | molecular_function | protein homodimerization activity |
| F | 0004364 | molecular_function | glutathione transferase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0006749 | biological_process | glutathione metabolic process |
| F | 0006805 | biological_process | xenobiotic metabolic process |
| F | 0016740 | molecular_function | transferase activity |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0042803 | molecular_function | protein homodimerization activity |
| G | 0004364 | molecular_function | glutathione transferase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0006749 | biological_process | glutathione metabolic process |
| G | 0006805 | biological_process | xenobiotic metabolic process |
| G | 0016740 | molecular_function | transferase activity |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0042803 | molecular_function | protein homodimerization activity |
| H | 0004364 | molecular_function | glutathione transferase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0006749 | biological_process | glutathione metabolic process |
| H | 0006805 | biological_process | xenobiotic metabolic process |
| H | 0016740 | molecular_function | transferase activity |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | GTA |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| A | TYR9 |
| A | ARG131 |
| A | PHE220 |
| A | ARG15 |
| A | LEU41 |
| A | GLN45 |
| A | GLN54 |
| A | VAL55 |
| A | GLN67 |
| A | THR68 |
| A | ASP101 |
| site_id | GTB |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| B | TYR9 |
| B | ARG15 |
| B | LEU41 |
| B | GLN45 |
| B | GLN54 |
| B | VAL55 |
| B | GLN67 |
| B | THR68 |
| B | ASP101 |
| B | ARG131 |
| B | PHE220 |
| site_id | GTC |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| C | TYR9 |
| C | ARG15 |
| C | LEU41 |
| C | GLN45 |
| C | GLN54 |
| C | VAL55 |
| C | GLN67 |
| C | THR68 |
| C | ASP101 |
| C | ARG131 |
| C | PHE220 |
| site_id | GTD |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| D | TYR9 |
| D | ARG15 |
| D | LEU41 |
| D | GLN45 |
| D | GLN54 |
| D | VAL55 |
| D | GLN67 |
| D | THR68 |
| D | ASP101 |
| D | ARG131 |
| D | PHE220 |
| site_id | GTE |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| E | TYR9 |
| E | ARG15 |
| E | LEU41 |
| E | GLN45 |
| E | GLN54 |
| E | VAL55 |
| E | GLN67 |
| E | THR68 |
| E | ASP101 |
| E | ARG131 |
| E | PHE220 |
| site_id | GTF |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| F | GLN54 |
| F | VAL55 |
| F | GLN67 |
| F | THR68 |
| F | ASP101 |
| F | ARG131 |
| F | PHE220 |
| F | TYR9 |
| F | ARG15 |
| F | LEU41 |
| F | GLN45 |
| site_id | GTG |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| G | TYR9 |
| G | ARG15 |
| G | LEU41 |
| G | GLN45 |
| G | GLN54 |
| G | VAL55 |
| G | GLN67 |
| G | THR68 |
| G | ASP101 |
| G | ARG131 |
| G | PHE220 |
| site_id | GTH |
| Number of Residues | 11 |
| Details | GLUTATHIONE BINDING SITE. |
| Chain | Residue |
| H | TYR9 |
| H | ARG15 |
| H | LEU41 |
| H | GLN45 |
| H | GLN54 |
| H | VAL55 |
| H | GLN67 |
| H | THR68 |
| H | ASP101 |
| H | ARG131 |
| H | PHE220 |
| site_id | HTA |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| A | GLY14 |
| A | GLU104 |
| A | ILE107 |
| A | MET108 |
| A | PHE111 |
| A | TYR212 |
| A | VAL216 |
| A | TYR217 |
| site_id | HTB |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| B | GLY14 |
| B | GLU104 |
| B | ILE107 |
| B | MET108 |
| B | PHE111 |
| B | TYR212 |
| B | VAL216 |
| B | TYR217 |
| site_id | HTC |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| C | GLY14 |
| C | GLU104 |
| C | ILE107 |
| C | MET108 |
| C | PHE111 |
| C | TYR212 |
| C | VAL216 |
| C | TYR217 |
| site_id | HTD |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| D | GLY14 |
| D | GLU104 |
| D | ILE107 |
| D | MET108 |
| D | PHE111 |
| D | TYR212 |
| D | VAL216 |
| D | TYR217 |
| site_id | HTE |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| E | GLY14 |
| E | GLU104 |
| E | ILE107 |
| E | MET108 |
| E | PHE111 |
| E | TYR212 |
| E | VAL216 |
| E | TYR217 |
| site_id | HTF |
| Number of Residues | 1 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| F | GLY14 |
| site_id | HTG |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| G | GLY14 |
| G | GLU104 |
| G | ILE107 |
| G | MET108 |
| G | PHE111 |
| G | TYR212 |
| G | VAL216 |
| G | TYR217 |
| site_id | HTH |
| Number of Residues | 8 |
| Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
| Chain | Residue |
| H | GLY14 |
| H | GLU104 |
| H | ILE107 |
| H | MET108 |
| H | PHE111 |
| H | TYR212 |
| H | VAL216 |
| H | TYR217 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13745 |
| Chain | Residue | Details |
| A | TYR9 | |
| E | GLN67 | |
| F | TYR9 | |
| F | GLN67 | |
| G | TYR9 | |
| G | GLN67 | |
| H | TYR9 | |
| H | GLN67 | |
| A | GLN67 | |
| B | TYR9 | |
| B | GLN67 | |
| C | TYR9 | |
| C | GLN67 | |
| D | TYR9 | |
| D | GLN67 | |
| E | TYR9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30711 |
| Chain | Residue | Details |
| A | GLN54 | |
| B | GLN54 | |
| C | GLN54 | |
| D | GLN54 | |
| E | GLN54 | |
| F | GLN54 | |
| G | GLN54 | |
| H | GLN54 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR212 | |
| B | TYR212 | |
| C | TYR212 | |
| D | TYR212 | |
| E | TYR212 | |
| F | TYR212 | |
| G | TYR212 | |
| H | TYR212 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P14942 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 | |
| C | MET1 | |
| D | MET1 | |
| E | MET1 | |
| F | MET1 | |
| G | MET1 | |
| H | MET1 |
