6DTP
CRYSTAL STRUCTURE OF HUMAN 17BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 1 COMPLEXED WITH EM139
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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)] activity |
| B | 0005496 | molecular_function | steroid binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0006703 | biological_process | estrogen biosynthetic process |
| B | 0007040 | biological_process | lysosome organization |
| B | 0007519 | biological_process | skeletal muscle tissue development |
| B | 0008210 | biological_process | estrogen metabolic process |
| B | 0010467 | biological_process | gene expression |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030283 | molecular_function | testosterone dehydrogenase [NAD(P)] activity |
| B | 0035410 | molecular_function | dihydrotestosterone 17-beta-dehydrogenase activity |
| B | 0036094 | molecular_function | small molecule binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
| B | 0047045 | molecular_function | testosterone 17-beta-dehydrogenase (NADP+) activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0060348 | biological_process | bone development |
| B | 0060612 | biological_process | adipose tissue development |
| B | 0061370 | biological_process | testosterone biosynthetic process |
| B | 0070401 | molecular_function | NADP+ binding |
| B | 0071248 | biological_process | cellular response to metal ion |
| B | 0072582 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| B | 1903924 | molecular_function | estradiol binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | PRO55 |
| A | PRO56 |
| A | GLY57 |
| A | SER58 |
| A | LEU59 |
| A | ALA230 |
| A | GLU235 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ARG266 |
| A | GOL404 |
| A | HOH514 |
| B | GLY145 |
| B | LEU146 |
| B | PHE160 |
| B | ARG266 |
| B | HOH506 |
| A | GLY145 |
| A | PHE160 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | ARG50 |
| A | VAL239 |
| A | THR242 |
| A | TYR253 |
| A | PHE254 |
| A | HOH502 |
| A | HOH505 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | ARG266 |
| A | ASP269 |
| A | PRO270 |
| A | GOL402 |
| B | LEU146 |
| B | ARG252 |
| B | HOH506 |
| B | HOH518 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | CYS89 |
| A | ASN90 |
| A | ALA91 |
| A | GLY92 |
| A | ASN114 |
| A | THR118 |
| A | LYS159 |
| A | LEU162 |
| A | HOH508 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ARG252 |
| A | HOH507 |
| A | HOH514 |
| B | ARG266 |
| B | PRO270 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASP25 |
| A | SER27 |
| A | ARG245 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue EM9 A 408 |
| Chain | Residue |
| A | SER142 |
| A | VAL143 |
| A | LEU149 |
| A | TYR155 |
| A | GLY186 |
| A | PRO187 |
| A | TYR218 |
| A | HIS221 |
| A | SER222 |
| A | PHE226 |
| A | PHE259 |
| A | MET279 |
| A | GLU282 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue PGE A 409 |
| Chain | Residue |
| A | ALA170 |
| A | LEU173 |
| A | LEU174 |
| A | VAL178 |
| A | LEU180 |
| A | PRO249 |
| A | THR250 |
| A | LEU251 |
| B | THR277 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | GLU47 |
| B | PHE254 |
| B | THR255 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | TRP46 |
| B | ARG50 |
| B | ALA230 |
| B | ASN232 |
| B | GLU235 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | TYR216 |
| B | LYS223 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | PHE125 |
| B | ASP128 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 405 |
| Chain | Residue |
| A | LYS130 |
| A | PRO175 |
| B | ARG214 |
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 | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR155 | |
| B | TYR155 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8805577 |
| Chain | Residue | Details |
| A | GLY9 | |
| A | ASP65 | |
| A | SER142 | |
| A | LYS159 | |
| B | GLY9 | |
| B | ASP65 | |
| B | SER142 | |
| B | LYS159 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:8994190 |
| Chain | Residue | Details |
| A | SER134 | |
| B | SER134 |
