3U3O
Crystal structure of Human SULT1A1 bound to PAP and two 3-Cyano-7-hydroxycoumarin
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 | 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 | 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 | 9 |
| Details | BINDING SITE FOR RESIDUE 3QV A 296 |
| Chain | Residue |
| A | PHE81 |
| A | LYS106 |
| A | HIS108 |
| A | VAL148 |
| A | PHE247 |
| A | MET248 |
| A | 3QV297 |
| A | HOH358 |
| A | HOH370 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 3QV A 297 |
| Chain | Residue |
| A | PHE76 |
| A | MET77 |
| A | PHE81 |
| A | PHE84 |
| A | ILE89 |
| A | PRO90 |
| A | PRO244 |
| A | 3QV296 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE A3P A 298 |
| Chain | Residue |
| A | LYS48 |
| A | SER49 |
| A | GLY50 |
| A | THR51 |
| A | THR52 |
| A | TRP53 |
| A | ARG130 |
| A | SER138 |
| A | TYR193 |
| A | THR227 |
| A | SER228 |
| A | PHE229 |
| A | MET232 |
| A | PHE255 |
| A | MET256 |
| A | ARG257 |
| A | LYS258 |
| A | GLY259 |
| A | HOH308 |
| A | HOH309 |
| A | HOH313 |
| A | HOH359 |
| A | HOH370 |
| A | HOH512 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS108 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673 |
| Chain | Residue | Details |
| A | LYS106 | |
| A | ARG130 | |
| A | SER138 | |
| A | TYR193 | |
| A | THR227 | |
| A | PHE255 | |
| A | LYS48 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17988 |
| Chain | Residue | Details |
| A | SER138 |
