1RAL
THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016229 | molecular_function | steroid dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0021766 | biological_process | hippocampus development |
| A | 0032052 | molecular_function | bile acid binding |
| A | 0042448 | biological_process | progesterone metabolic process |
| A | 0044597 | biological_process | daunorubicin metabolic process |
| A | 0044598 | biological_process | doxorubicin metabolic process |
| A | 0047023 | molecular_function | androsterone dehydrogenase activity |
| A | 0047042 | molecular_function | androsterone dehydrogenase (B-specific) activity |
| A | 0047086 | molecular_function | ketosteroid monooxygenase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglAKSIGVSNF |
| Chain | Residue | Details |
| A | MET151-PHE168 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LIRSFNakRIkELtQV |
| Chain | Residue | Details |
| A | LEU268-VAL283 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GFRHFDSAylyevEeeVG |
| Chain | Residue | Details |
| A | GLY45-GLY62 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | TYR55 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9261071 |
| Chain | Residue | Details |
| A | GLY20 | |
| A | ASP50 | |
| A | SER166 | |
| A | GLN190 | |
| A | TYR216 | |
| A | ARG270 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS117 | |
| A | TRP227 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS84 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Blocked amino end (Met) |
| Chain | Residue | Details |
| A | MET1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS84 | |
| A | HIS117 | |
| A | ASP50 | |
| A | TYR55 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mrq |
| Chain | Residue | Details |
| A | LYS84 | |
| A | TYR55 |
