1Q1Q
Crystal structure of human pregnenolone sulfotransferase (SULT2B1a) in the presence of PAP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004027 | molecular_function | alcohol sulfotransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008146 | molecular_function | sulfotransferase activity |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008285 | biological_process | negative regulation of cell population proliferation |
| A | 0015485 | molecular_function | cholesterol binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0045606 | biological_process | positive regulation of epidermal cell differentiation |
| A | 0050294 | molecular_function | steroid sulfotransferase activity |
| A | 0050427 | biological_process | 3'-phosphoadenosine 5'-phosphosulfate metabolic process |
| A | 0051922 | molecular_function | cholesterol sulfotransferase activity |
| A | 0051923 | biological_process | sulfation |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1990239 | molecular_function | steroid hormone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 351 |
| Chain | Residue |
| A | SER145 |
| A | ALA148 |
| A | LEU151 |
| A | ASP153 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE A3P A 352 |
| Chain | Residue |
| A | TRP60 |
| A | ARG132 |
| A | SER140 |
| A | TYR195 |
| A | GLN199 |
| A | SER229 |
| A | PHE231 |
| A | MET234 |
| A | PHE257 |
| A | LEU258 |
| A | ARG259 |
| A | LYS260 |
| A | GLY261 |
| A | LYS55 |
| A | SER56 |
| A | GLY57 |
| A | THR58 |
| A | THR59 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NHE A 353 |
| Chain | Residue |
| A | TYR142 |
| A | PRO157 |
| A | LEU161 |
| A | HIS269 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NHE A 354 |
| Chain | Residue |
| A | TYR29 |
| A | PRO54 |
| A | TRP88 |
| A | TYR144 |
| A | GLN150 |
| A | GLN170 |
| A | PHE171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P49891 |
| Chain | Residue | Details |
| A | HIS110 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P49891 |
| Chain | Residue | Details |
| A | LYS55 | |
| A | ARG132 | |
| A | SER140 | |
| A | TYR195 | |
| A | SER229 | |
| A | ARG259 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TRP83 | |
| A | TRP88 | |
| A | HIS110 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:21855633 |
| Chain | Residue | Details |
| A | SER333 |
