6GSU
FIRST-SPHERE AND SECOND-SPHERE ELECTROSTATIC EFFECTS IN THE ACTIVE SITE OF A CLASS MU GLUTATHIONE TRANSFERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005496 | molecular_function | steroid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0010038 | biological_process | response to metal ion |
| A | 0010288 | biological_process | response to lead ion |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042178 | biological_process | xenobiotic catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043200 | biological_process | response to amino acid |
| A | 0043295 | molecular_function | glutathione binding |
| A | 0045471 | biological_process | response to ethanol |
| A | 0048678 | biological_process | response to axon injury |
| A | 0051122 | biological_process | hepoxilin biosynthetic process |
| A | 1901687 | biological_process | glutathione derivative biosynthetic process |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0005496 | molecular_function | steroid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0010038 | biological_process | response to metal ion |
| B | 0010288 | biological_process | response to lead ion |
| B | 0016151 | molecular_function | nickel cation binding |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042178 | biological_process | xenobiotic catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043200 | biological_process | response to amino acid |
| B | 0043295 | molecular_function | glutathione binding |
| B | 0045471 | biological_process | response to ethanol |
| B | 0048678 | biological_process | response to axon injury |
| B | 0051122 | biological_process | hepoxilin biosynthetic process |
| B | 1901687 | biological_process | glutathione derivative biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GPS A 221 |
| Chain | Residue |
| A | TYR6 |
| A | SER72 |
| A | MET108 |
| A | ILE111 |
| A | PHE208 |
| B | ASP105 |
| A | HOH223 |
| A | HOH236 |
| A | HOH270 |
| A | HOH307 |
| A | HOH311 |
| A | TRP7 |
| A | HOH326 |
| A | HOH345 |
| A | HOH388 |
| A | GLY11 |
| A | LEU12 |
| A | TRP45 |
| A | LYS49 |
| A | ASN58 |
| A | LEU59 |
| A | GLN71 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GPS B 218 |
| Chain | Residue |
| A | ASP105 |
| B | TYR6 |
| B | TRP7 |
| B | GLY11 |
| B | LEU12 |
| B | TRP45 |
| B | LYS49 |
| B | ASN58 |
| B | LEU59 |
| B | GLN71 |
| B | SER72 |
| B | MET108 |
| B | ILE111 |
| B | PHE208 |
| B | HOH219 |
| B | HOH220 |
| A | HOH244 |
| B | HOH274 |
| B | HOH292 |
| B | HOH297 |
| B | HOH305 |
| B | HOH312 |
| B | HOH323 |
| B | HOH336 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 218 |
| Chain | Residue |
| A | ARG201 |
| A | HOH292 |
| A | HOH330 |
| A | HOH385 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 219 |
| Chain | Residue |
| A | ASP105 |
| A | GLN109 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 220 |
| Chain | Residue |
| A | HOH310 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 172 |
| Details | Domain: {"description":"GST N-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 236 |
| Details | Domain: {"description":"GST C-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8664265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8110735","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| A | TYR6 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oe8 |
| Chain | Residue | Details |
| B | TYR6 |
