4JVM
Crystal structure of human estrogen sulfotransferase (SULT1E1) in complex with inactive cofactor PAP and brominated flame retardant TBBPA (tetrabromobisphenol A)
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 | 0008146 | molecular_function | sulfotransferase activity |
A | 0008202 | biological_process | steroid metabolic process |
A | 0008210 | biological_process | estrogen metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0031965 | cellular_component | nuclear membrane |
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 | 0008146 | molecular_function | sulfotransferase activity |
B | 0008202 | biological_process | steroid metabolic process |
B | 0008210 | biological_process | estrogen metabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0031965 | cellular_component | nuclear membrane |
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 | 11 |
Details | BINDING SITE FOR RESIDUE XDI A 501 |
Chain | Residue |
A | PHE23 |
A | ILE246 |
A | HOH627 |
A | PHE80 |
A | CYS83 |
A | LYS85 |
A | MET89 |
A | LYS105 |
A | HIS107 |
A | VAL145 |
A | TYR239 |
site_id | AC2 |
Number of Residues | 22 |
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 | SER227 |
A | PHE228 |
A | MET231 |
A | PHE254 |
A | MET255 |
A | ARG256 |
A | LYS257 |
A | GLY258 |
A | HOH614 |
A | HOH621 |
A | HOH624 |
A | HOH627 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 503 |
Chain | Residue |
A | GLY182 |
A | SER184 |
A | VAL187 |
A | HOH758 |
A | HOH785 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | ASP194 |
A | LYS201 |
A | GLU202 |
A | LYS205 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | LYS132 |
A | ASP276 |
A | TYR279 |
A | THR292 |
A | HOH700 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE XDI B 301 |
Chain | Residue |
B | PHE75 |
B | PHE80 |
B | MET89 |
B | LYS105 |
B | HIS107 |
B | VAL145 |
B | TYR239 |
B | HOH411 |
site_id | AC7 |
Number of Residues | 24 |
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 | SER227 |
B | PHE228 |
B | MET231 |
B | PHE254 |
B | MET255 |
B | ARG256 |
B | LYS257 |
B | GLY258 |
B | HOH406 |
B | HOH411 |
B | HOH412 |
B | HOH449 |
B | HOH468 |
B | HOH646 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 303 |
Chain | Residue |
B | GLY182 |
B | SER184 |
B | VAL187 |
B | HOH426 |
B | HOH438 |
B | HOH471 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
B | LYS132 |
B | PHE275 |
B | ASP276 |
B | TYR279 |
B | THR292 |
B | HOH422 |
B | HOH459 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 305 |
Chain | Residue |
B | ASP194 |
B | LYS201 |
B | GLU202 |
B | LYS205 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 306 |
Chain | Residue |
B | HOH583 |
B | HOH620 |
B | HOH621 |
B | TYR8 |
B | PHE11 |
B | HOH556 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11006110 |
Chain | Residue | Details |
A | HIS107 | |
B | HIS107 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P49891 |
Chain | Residue | Details |
A | LYS47 | |
B | TYR192 | |
B | THR226 | |
B | ARG256 | |
A | LYS105 | |
A | ARG129 | |
A | TYR192 | |
A | THR226 | |
A | ARG256 | |
B | LYS47 | |
B | LYS105 | |
B | ARG129 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11884392 |
Chain | Residue | Details |
A | SER137 | |
B | SER137 |
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 |