5YVO
Human Glutathione Transferase Omega1 covalently bound to ML175 inhibitor
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 | 8 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | GLU21 |
| A | GLY22 |
| A | SER78 |
| A | GLN79 |
| A | HOH431 |
| A | HOH452 |
| A | HOH467 |
| A | HOH488 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | HIS49 |
| A | HOH410 |
| A | HOH411 |
| A | HOH477 |
| A | HOH480 |
| A | HOH540 |
| A | ARG39 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | ARG30 |
| A | LYS136 |
| A | HOH405 |
| A | HOH411 |
| A | HOH434 |
| A | HOH480 |
| A | HOH493 |
| A | HOH517 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | GLU91 |
| A | LEU117 |
| A | LEU176 |
| A | HOH527 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue MLX A 305 |
| Chain | Residue |
| A | MET29 |
| A | CYS32 |
| A | PRO33 |
| A | PHE34 |
| A | LEU56 |
| A | LYS57 |
| A | VAL127 |
| A | GLY128 |
| A | TRP222 |
| A | TYR229 |
| A | HOH439 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue MLX A 306 |
| Chain | Residue |
| A | GLU4 |
| A | SER5 |
| A | ARG7 |
| A | LYS65 |
| A | LYS66 |
| A | LEU82 |
| A | TYR84 |
| A | TYR108 |
| A | CYS112 |
| A | GLU155 |
| A | ASN159 |
| A | LYS160 |
| A | HOH539 |
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 |
