1B4P
CRYSTAL STRUCTURES OF CLASS MU CHIMERIC GST ISOENZYMES M1-2 AND M2-1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0004602 | molecular_function | glutathione peroxidase activity |
A | 0005102 | molecular_function | signaling receptor binding |
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 | 0006749 | biological_process | glutathione metabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0007608 | biological_process | sensory perception of smell |
A | 0010038 | biological_process | response to metal ion |
A | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
A | 0014070 | biological_process | response to organic cyclic compound |
A | 0016529 | cellular_component | sarcoplasmic reticulum |
A | 0016740 | molecular_function | transferase activity |
A | 0018916 | biological_process | nitrobenzene metabolic process |
A | 0019899 | molecular_function | enzyme binding |
A | 0032991 | cellular_component | protein-containing complex |
A | 0033595 | biological_process | response to genistein |
A | 0042178 | biological_process | xenobiotic catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043295 | molecular_function | glutathione binding |
A | 0043651 | biological_process | linoleic acid metabolic process |
A | 0050896 | biological_process | response to stimulus |
A | 0051122 | biological_process | hepoxilin biosynthetic process |
A | 0070458 | biological_process | cellular detoxification of nitrogen compound |
A | 0071313 | biological_process | cellular response to caffeine |
A | 0098869 | biological_process | cellular oxidant detoxification |
A | 1902168 | biological_process | response to catechin |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 221 |
Chain | Residue |
A | ARG167 |
A | HOH391 |
A | HOH475 |
A | HOH521 |
A | HOH535 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 222 |
Chain | Residue |
A | LEU52 |
A | ILE63 |
A | LYS68 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 223 |
Chain | Residue |
A | LYS135 |
A | PHE202 |
A | LEU203 |
A | SER204 |
A | LYS205 |
A | HOH395 |
A | HOH497 |
A | HOH526 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE GPS A 218 |
Chain | Residue |
A | TYR6 |
A | TRP7 |
A | VAL9 |
A | GLY11 |
A | LEU12 |
A | ARG42 |
A | TRP45 |
A | LYS49 |
A | ASN58 |
A | LEU59 |
A | GLN71 |
A | SER72 |
A | ASP105 |
A | TYR115 |
A | PHE208 |
A | ALA209 |
A | HOH301 |
A | HOH302 |
A | HOH325 |
A | HOH386 |
A | HOH415 |
A | HOH508 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GPS A 219 |
Chain | Residue |
A | LEU20 |
A | GLU21 |
A | ASP24 |
A | SER25 |
A | SER26 |
A | TYR27 |
A | GLU28 |
A | GLU29 |
A | PRO131 |
A | LYS172 |
A | CYS173 |
A | ALA176 |
A | ARG201 |
A | HOH384 |
A | HOH429 |
A | HOH533 |
site_id | GPS |
Number of Residues | 1 |
Details | NON3 |
Chain | Residue |
A | TYR6 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000305|PubMed:8664265 |
Chain | Residue | Details |
A | ARG42 | |
A | LYS49 | |
A | ASN58 | |
A | GLN71 | |
A | TYR6 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | TYR115 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER26 | |
A | SER43 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P15626 |
Chain | Residue | Details |
A | SER116 |