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 | 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 | 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 | 0008289 | molecular_function | lipid binding |
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 | 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 | 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 |