4JVN
Crystal structure of human estrogen sulfotransferase (SULT1E1) in complex with inactive cofactor PAP and metabolite of brominated flame retardant 3OH BDE47 (3-hydroxyl bromodiphenyl ether)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004062 | molecular_function | aryl sulfotransferase activity |
| A | 0004304 | molecular_function | estrone sulfotransferase activity |
| A | 0005496 | molecular_function | steroid binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006068 | biological_process | ethanol catabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006711 | biological_process | estrogen catabolic process |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0008146 | molecular_function | sulfotransferase activity |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008210 | biological_process | estrogen metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0045600 | biological_process | positive regulation of fat cell differentiation |
| 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 | 0051923 | biological_process | sulfation |
| B | 0004062 | molecular_function | aryl sulfotransferase activity |
| B | 0004304 | molecular_function | estrone sulfotransferase activity |
| B | 0005496 | molecular_function | steroid binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006068 | biological_process | ethanol catabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006711 | biological_process | estrogen catabolic process |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0008146 | molecular_function | sulfotransferase activity |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008210 | biological_process | estrogen metabolic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0045600 | biological_process | positive regulation of fat cell differentiation |
| B | 0047894 | molecular_function | flavonol 3-sulfotransferase activity |
| B | 0050294 | molecular_function | steroid sulfotransferase activity |
| B | 0050427 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate metabolic process |
| B | 0051923 | biological_process | sulfation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE YUG A 501 |
| Chain | Residue |
| A | TYR20 |
| A | PHE80 |
| A | CYS83 |
| A | LYS105 |
| A | HIS107 |
| A | PHE141 |
| A | VAL145 |
| A | ILE246 |
| A | HOH618 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE A3P A 502 |
| Chain | Residue |
| A | LYS47 |
| A | SER48 |
| A | GLY49 |
| A | THR50 |
| A | THR51 |
| A | TRP52 |
| A | ARG129 |
| A | SER137 |
| A | TYR192 |
| A | THR226 |
| A | PHE228 |
| A | MET231 |
| A | PHE254 |
| A | MET255 |
| A | ARG256 |
| A | LYS257 |
| A | GLY258 |
| A | HOH618 |
| A | HOH624 |
| A | HOH636 |
| A | HOH637 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 503 |
| Chain | Residue |
| A | GLY182 |
| A | SER184 |
| A | VAL187 |
| A | HOH803 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE YUG B 301 |
| Chain | Residue |
| B | PHE80 |
| B | LYS105 |
| B | HIS107 |
| B | PHE141 |
| B | TYR239 |
| B | HOH412 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE A3P B 302 |
| Chain | Residue |
| B | LYS47 |
| B | SER48 |
| B | GLY49 |
| B | THR50 |
| B | THR51 |
| B | TRP52 |
| B | ARG129 |
| B | SER137 |
| B | TYR192 |
| B | THR226 |
| B | PHE228 |
| B | MET231 |
| B | PHE254 |
| B | MET255 |
| B | ARG256 |
| B | LYS257 |
| B | GLY258 |
| B | HOH412 |
| B | HOH415 |
| B | HOH422 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| B | ASP194 |
| B | LYS201 |
| B | GLU202 |
| B | LYS205 |
| B | HOH592 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 304 |
| Chain | Residue |
| B | GLY182 |
| B | SER184 |
| B | VAL187 |
| B | HOH421 |
| B | HOH427 |
| B | HOH567 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 305 |
| Chain | Residue |
| B | LYS132 |
| B | ASP276 |
| B | TYR279 |
| B | THR292 |
| B | HOH419 |
| B | HOH488 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11006110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P49891","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11884392","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 154 |
| Chain | Residue | Details |
| A | LYS47 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS107 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
| A | SER137 | hydrogen bond acceptor, steric role |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 154 |
| Chain | Residue | Details |
| B | LYS47 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS107 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
| B | SER137 | hydrogen bond acceptor, steric role |
