1Z28
Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004062 | molecular_function | aryl sulfotransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006068 | biological_process | ethanol catabolic process |
| A | 0006584 | biological_process | catecholamine metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008146 | molecular_function | sulfotransferase activity |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008210 | biological_process | estrogen metabolic process |
| A | 0009308 | biological_process | amine metabolic process |
| A | 0009812 | biological_process | flavonoid metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042403 | biological_process | thyroid hormone metabolic process |
| A | 0042420 | biological_process | dopamine catabolic process |
| A | 0047894 | molecular_function | flavonol 3-sulfotransferase activity |
| A | 0050294 | molecular_function | steroid sulfotransferase activity |
| A | 0050427 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate metabolic process |
| A | 0050656 | molecular_function | 3'-phosphoadenosine 5'-phosphosulfate binding |
| A | 0051923 | biological_process | sulfation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE A3P A 1001 |
| Chain | Residue |
| A | LYS48 |
| A | THR227 |
| A | SER228 |
| A | PHE229 |
| A | MET232 |
| A | PHE255 |
| A | MET256 |
| A | ARG257 |
| A | LYS258 |
| A | GLY259 |
| A | HOH1005 |
| A | SER49 |
| A | HOH1014 |
| A | HOH1015 |
| A | HOH1031 |
| A | HOH1045 |
| A | GLY50 |
| A | THR51 |
| A | THR52 |
| A | TRP53 |
| A | ARG130 |
| A | SER138 |
| A | TYR193 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0DMM9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12471039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16221673","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P17988","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
