6OW4
Structure of the NADH-bound form of 20beta-Hydroxysteroid Dehydrogenase from Bifidobacterium adolescentis strain L2-32
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY48 |
| A | ASN128 |
| A | ALA129 |
| A | GLY130 |
| A | VAL131 |
| A | THR179 |
| A | ALA181 |
| A | TYR200 |
| A | LYS204 |
| A | PRO230 |
| A | GLY231 |
| A | GLY51 |
| A | VAL233 |
| A | SER235 |
| A | ILE237 |
| A | PHE238 |
| A | HOH432 |
| A | GLY52 |
| A | LEU53 |
| A | ASP72 |
| A | LEU73 |
| A | CYS100 |
| A | ASP101 |
| A | VAL102 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY48 |
| B | ALA50 |
| B | GLY51 |
| B | GLY52 |
| B | LEU53 |
| B | ASP72 |
| B | LEU73 |
| B | CYS100 |
| B | ASP101 |
| B | VAL102 |
| B | ASN128 |
| B | ALA129 |
| B | GLY130 |
| B | VAL131 |
| B | THR179 |
| B | TYR200 |
| B | LYS204 |
| B | PRO230 |
| B | GLY231 |
| B | VAL233 |
| B | SER235 |
| B | ILE237 |
| B | PHE238 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue NAD C 301 |
| Chain | Residue |
| C | GLY48 |
| C | ALA50 |
| C | GLY51 |
| C | GLY52 |
| C | LEU53 |
| C | ASP72 |
| C | LEU73 |
| C | CYS100 |
| C | ASP101 |
| C | VAL102 |
| C | ASN128 |
| C | GLY130 |
| C | ILE151 |
| C | THR179 |
| C | ALA180 |
| C | ALA181 |
| C | TYR200 |
| C | LYS204 |
| C | PRO230 |
| C | GLY231 |
| C | VAL233 |
| C | SER235 |
| C | ILE237 |
| C | PHE238 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue NAD D 301 |
| Chain | Residue |
| D | GLY48 |
| D | GLY51 |
| D | GLY52 |
| D | LEU53 |
| D | ASP72 |
| D | LEU73 |
| D | CYS100 |
| D | ASP101 |
| D | VAL102 |
| D | ASN128 |
| D | ALA129 |
| D | GLY130 |
| D | VAL131 |
| D | THR179 |
| D | ALA180 |
| D | ALA181 |
| D | TYR200 |
| D | LYS204 |
| D | PRO230 |
| D | GLY231 |
| D | VAL233 |
| D | SER235 |
| D | ILE237 |
| D | PHE238 |
| D | HOH437 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue NAD E 301 |
| Chain | Residue |
| E | LEU53 |
| E | ASP72 |
| E | LEU73 |
| E | CYS100 |
| E | ASP101 |
| E | VAL102 |
| E | ASN128 |
| E | ALA129 |
| E | GLY130 |
| E | ILE151 |
| E | THR179 |
| E | ALA180 |
| E | ALA181 |
| E | TYR200 |
| E | LYS204 |
| E | PRO230 |
| E | GLY231 |
| E | VAL233 |
| E | SER235 |
| E | ILE237 |
| E | GLY48 |
| E | GLY51 |
| E | GLY52 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for residue NAD F 301 |
| Chain | Residue |
| F | GLY48 |
| F | GLY51 |
| F | GLY52 |
| F | LEU53 |
| F | ASP72 |
| F | LEU73 |
| F | CYS100 |
| F | ASP101 |
| F | VAL102 |
| F | ASN128 |
| F | ALA129 |
| F | GLY130 |
| F | ILE151 |
| F | THR179 |
| F | ALA180 |
| F | ALA181 |
| F | TYR200 |
| F | LYS204 |
| F | PRO230 |
| F | GLY231 |
| F | VAL233 |
| F | SER235 |
| F | ILE237 |
| F | HOH415 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue NAD G 301 |
| Chain | Residue |
| G | GLY48 |
| G | GLY51 |
| G | GLY52 |
| G | LEU53 |
| G | ASP72 |
| G | LEU73 |
| G | CYS100 |
| G | ASP101 |
| G | VAL102 |
| G | ASN128 |
| G | ALA129 |
| G | GLY130 |
| G | VAL131 |
| G | THR179 |
| G | ALA180 |
| G | ALA181 |
| G | TYR200 |
| G | LYS204 |
| G | PRO230 |
| G | GLY231 |
| G | VAL233 |
| G | SER235 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | binding site for residue NAD H 301 |
| Chain | Residue |
| H | GLY48 |
| H | GLY51 |
| H | GLY52 |
| H | LEU53 |
| H | ASP72 |
| H | LEU73 |
| H | CYS100 |
| H | ASP101 |
| H | VAL102 |
| H | ASN128 |
| H | ALA129 |
| H | GLY130 |
| H | VAL131 |
| H | ILE151 |
| H | THR179 |
| H | ALA180 |
| H | ALA181 |
| H | TYR200 |
| H | LYS204 |
| H | PRO230 |
| H | GLY231 |
| H | VAL233 |
| H | SER235 |
| H | ILE237 |
| H | PHE238 |
| H | HOH412 |
| H | HOH424 |
