1EEM
GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS
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 | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
A | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
A | 0014810 | biological_process | positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0019852 | biological_process | L-ascorbic acid metabolic process |
A | 0042178 | biological_process | xenobiotic catabolic process |
A | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
A | 0050610 | molecular_function | methylarsonate reductase activity |
A | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
A | 0060316 | biological_process | positive regulation of ryanodine-sensitive calcium-release channel activity |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071243 | biological_process | cellular response to arsenic-containing substance |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 901 |
Chain | Residue |
A | ARG39 |
A | HIS49 |
A | VAL51 |
A | HOH1009 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 902 |
Chain | Residue |
A | HOH1137 |
A | GLU21 |
A | GLY22 |
A | SER78 |
A | GLN79 |
A | HOH1021 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GSH A 999 |
Chain | Residue |
A | CYS32 |
A | PHE34 |
A | LEU56 |
A | LYS59 |
A | LEU71 |
A | VAL72 |
A | PRO73 |
A | GLU85 |
A | SER86 |
A | HOH1002 |
A | HOH1030 |
A | HOH1043 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:10783391 |
Chain | Residue | Details |
A | CYS32 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529 |
Chain | Residue | Details |
A | LYS59 | |
A | VAL72 | |
A | GLU85 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | SER2 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS57 | |
A | LYS143 | |
A | LYS148 | |
A | LYS152 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER129 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
A | SER28 |