1I5R
TYPE 1 17-BETA HYDROXYSTEROID DEHYDROGENASE EM1745 COMPLEX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)] activity |
| A | 0005496 | molecular_function | steroid binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006703 | biological_process | estrogen biosynthetic process |
| A | 0007040 | biological_process | lysosome organization |
| A | 0007519 | biological_process | skeletal muscle tissue development |
| A | 0008210 | biological_process | estrogen metabolic process |
| A | 0010467 | biological_process | gene expression |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030283 | molecular_function | testosterone dehydrogenase [NAD(P)] activity |
| A | 0035410 | molecular_function | dihydrotestosterone 17-beta-dehydrogenase activity |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
| A | 0047045 | molecular_function | testosterone 17-beta-dehydrogenase (NADP+) activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0060348 | biological_process | bone development |
| A | 0060612 | biological_process | adipose tissue development |
| A | 0061370 | biological_process | testosterone biosynthetic process |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 0071248 | biological_process | cellular response to metal ion |
| A | 0072582 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| A | 1903924 | molecular_function | estradiol binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE HYC A 328 |
| Chain | Residue |
| A | GLY9 |
| A | ALA91 |
| A | GLY92 |
| A | LEU93 |
| A | GLY94 |
| A | SER142 |
| A | MET147 |
| A | LEU149 |
| A | TYR155 |
| A | PHE192 |
| A | MET193 |
| A | SER11 |
| A | TYR218 |
| A | HIS221 |
| A | SER222 |
| A | PHE226 |
| A | PHE259 |
| A | MET279 |
| A | GLU282 |
| A | GOL401 |
| A | HOH410 |
| A | HOH430 |
| A | SER12 |
| A | HOH489 |
| A | HOH557 |
| A | ARG37 |
| A | LEU64 |
| A | ASP65 |
| A | VAL66 |
| A | ARG67 |
| A | ASN90 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 401 |
| Chain | Residue |
| A | GLY186 |
| A | PRO187 |
| A | VAL188 |
| A | PHE192 |
| A | PHE226 |
| A | HYC328 |
| A | HOH438 |
| A | HOH621 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | LEU146 |
| A | ARG252 |
| A | PHE254 |
| A | ARG266 |
| A | ASP269 |
| A | PRO270 |
| A | GOL403 |
| A | GOL403 |
| A | HOH416 |
| A | HOH452 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | GLY145 |
| A | GLY145 |
| A | LEU146 |
| A | PHE160 |
| A | PHE160 |
| A | GLU163 |
| A | GLU163 |
| A | ARG266 |
| A | GOL402 |
| A | GOL402 |
| A | HOH416 |
| A | HOH416 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvgglmglpfNdvYCASKFALeGLCeSLA |
| Chain | Residue | Details |
| A | SER142-ALA170 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | CYS156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8805577 |
| Chain | Residue | Details |
| A | CYS10 | |
| A | VAL66 | |
| A | VAL143 | |
| A | PHE160 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:8994190 |
| Chain | Residue | Details |
| A | GLY135 |
