2HSD
THE REFINED THREE-DIMENSIONAL STRUCTURE OF 3ALPHA,20BETA-HYDROXYSTEROID DEHYDROGENASE AND POSSIBLE ROLES OF THE RESIDUES CONSERVED IN SHORT-CHAIN DEHYDROGENASES
Replaces: 1HSDFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008207 | biological_process | C21-steroid hormone metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008207 | biological_process | C21-steroid hormone metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0008207 | biological_process | C21-steroid hormone metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0008207 | biological_process | C21-steroid hormone metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD A 256 |
| Chain | Residue |
| A | GLY13 |
| A | ASP60 |
| A | VAL61 |
| A | ASN87 |
| A | ALA88 |
| A | GLY89 |
| A | ILE137 |
| A | SER138 |
| A | SER139 |
| A | TYR152 |
| A | LYS156 |
| A | ARG16 |
| A | PRO182 |
| A | GLY183 |
| A | THR185 |
| A | GLY17 |
| A | LEU18 |
| A | GLY19 |
| A | ASP37 |
| A | VAL38 |
| A | LEU39 |
| A | LEU59 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 256 |
| Chain | Residue |
| B | GLY13 |
| B | ARG16 |
| B | GLY17 |
| B | LEU18 |
| B | ASP37 |
| B | VAL38 |
| B | LEU39 |
| B | LEU59 |
| B | ASP60 |
| B | VAL61 |
| B | ASN87 |
| B | ALA88 |
| B | GLY89 |
| B | ILE110 |
| B | ILE137 |
| B | SER139 |
| B | TYR152 |
| B | LYS156 |
| B | PRO182 |
| B | GLY183 |
| B | THR185 |
| B | THR190 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD C 256 |
| Chain | Residue |
| C | GLY13 |
| C | ARG16 |
| C | LEU18 |
| C | ASP37 |
| C | LEU39 |
| C | LEU59 |
| C | ASP60 |
| C | VAL61 |
| C | ASN87 |
| C | ALA88 |
| C | GLY89 |
| C | ILE110 |
| C | ILE137 |
| C | SER138 |
| C | SER139 |
| C | TYR152 |
| C | LYS156 |
| C | PRO182 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD D 256 |
| Chain | Residue |
| D | ARG16 |
| D | GLY17 |
| D | LEU18 |
| D | ASP37 |
| D | VAL38 |
| D | LEU39 |
| D | LEU59 |
| D | ASP60 |
| D | VAL61 |
| D | ASN87 |
| D | ALA88 |
| D | GLY89 |
| D | TYR152 |
| D | LYS156 |
| D | GLY183 |
| D | THR187 |
| D | MET189 |
| D | THR190 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SaaglmglalTssYGASKWGVrGLSkLAA |
| Chain | Residue | Details |
| A | SER139-ALA167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 96 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LEU143 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS156 | |
| A | THR149 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS156 | |
| B | THR149 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS156 | |
| C | THR149 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS156 | |
| D | THR149 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR152 | |
| C | LYS156 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR152 | |
| D | LYS156 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR152 | |
| C | LYS156 | |
| C | SER139 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR152 | |
| D | LYS156 | |
| D | SER139 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN111 | |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASN111 | |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASN111 | |
| C | TYR152 | |
| C | LYS156 | |
| C | SER139 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASN111 | |
| D | TYR152 | |
| D | LYS156 | |
| D | SER139 |
