1G3M
CRYSTAL STRUCTURE OF HUMAN ESTROGEN SULFOTRANSFERASE IN COMPLEX WITH IN-ACTIVE COFACTOR PAP AND 3,5,3',5'-TETRACHLORO-BIPHENYL-4,4'-DIOL
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 | 24 |
| Details | BINDING SITE FOR RESIDUE A3P A 701 |
| Chain | Residue |
| A | LYS47 |
| A | THR226 |
| A | SER227 |
| A | PHE228 |
| A | MET231 |
| A | PHE254 |
| A | MET255 |
| A | ARG256 |
| A | LYS257 |
| A | GLY258 |
| A | HOH811 |
| A | SER48 |
| A | HOH815 |
| A | HOH827 |
| A | HOH835 |
| A | HOH868 |
| A | HOH899 |
| A | GLY49 |
| A | THR50 |
| A | THR51 |
| A | TRP52 |
| A | ARG129 |
| A | SER137 |
| A | TYR192 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE A3P B 702 |
| 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 | HOH720 |
| B | HOH726 |
| B | HOH728 |
| B | HOH733 |
| B | HOH761 |
| B | HOH792 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PCQ B 711 |
| Chain | Residue |
| B | TYR20 |
| B | PHE80 |
| B | LYS105 |
| B | HIS107 |
| B | PHE141 |
| B | VAL145 |
| B | ALA146 |
| B | TYR239 |
| B | ILE246 |
| B | HOH733 |
| B | HOH996 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PCQ A 712 |
| Chain | Residue |
| A | TYR20 |
| A | PHE80 |
| A | LYS105 |
| A | HIS107 |
| A | PHE141 |
| A | VAL145 |
| A | ALA146 |
| A | ILE246 |
| A | HOH827 |
| A | HOH1120 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 801 |
| Chain | Residue |
| A | LYS25 |
| B | GLN163 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 802 |
| Chain | Residue |
| A | TYR8 |
| A | LEU18 |
| A | HOH891 |
| A | HOH976 |
| A | HOH1060 |
| B | GLU111 |
| B | SER177 |
| B | HOH798 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 803 |
| Chain | Residue |
| A | SER177 |
| A | HOH896 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 804 |
| Chain | Residue |
| A | ASN233 |
| A | HOH885 |
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 |
