1JTV
Crystal structure of 17beta-Hydroxysteroid Dehydrogenase Type 1 complexed with Testosterone
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 | 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 | 9 |
| Details | BINDING SITE FOR RESIDUE TES A 500 |
| Chain | Residue |
| A | VAL143 |
| A | TYR218 |
| A | HIS221 |
| A | SER222 |
| A | VAL225 |
| A | PHE259 |
| A | GLU282 |
| A | HOH647 |
| A | HOH716 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 600 |
| Chain | Residue |
| A | ARG252 |
| A | ARG266 |
| A | ASP269 |
| A | PRO270 |
| A | HOH607 |
| A | HOH618 |
| A | HOH624 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | ASN152 | |
| A | LYS159 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | TYR155 | |
| A | LYS159 |
