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 | 0008202 | biological_process | steroid metabolic process |
A | 0008207 | biological_process | C21-steroid hormone metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase activity |
B | 0008202 | biological_process | steroid metabolic process |
B | 0008207 | biological_process | C21-steroid hormone metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase activity |
C | 0008202 | biological_process | steroid metabolic process |
C | 0008207 | biological_process | C21-steroid hormone metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase activity |
D | 0008202 | biological_process | steroid metabolic process |
D | 0008207 | biological_process | C21-steroid hormone metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase 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 | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR152 | |
B | TYR152 | |
C | TYR152 | |
D | TYR152 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ILE10 | |
B | ILE10 | |
C | ILE10 | |
D | ILE10 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER139 | |
B | SER139 | |
C | SER139 | |
D | SER139 |
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 |