1EE2
THE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042573 | biological_process | retinoic acid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042573 | biological_process | retinoic acid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1300 |
| Chain | Residue |
| A | CYS46 |
| A | HIS67 |
| A | CYS173 |
| A | NAD1100 |
| A | CHD1150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1301 |
| Chain | Residue |
| A | CYS97 |
| A | CYS100 |
| A | CYS103 |
| A | CYS111 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1302 |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS173 |
| B | NAD1200 |
| B | CHD1250 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1303 |
| Chain | Residue |
| B | CYS97 |
| B | CYS100 |
| B | CYS103 |
| B | CYS111 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 1100 |
| Chain | Residue |
| A | ARG47 |
| A | SER48 |
| A | HIS51 |
| A | CYS173 |
| A | THR177 |
| A | GLY198 |
| A | GLY200 |
| A | GLY201 |
| A | VAL202 |
| A | ASP222 |
| A | ILE223 |
| A | LYS227 |
| A | VAL267 |
| A | ILE268 |
| A | ARG270 |
| A | VAL291 |
| A | GLY292 |
| A | VAL293 |
| A | ALA316 |
| A | ILE317 |
| A | PHE318 |
| A | LEU361 |
| A | ARG368 |
| A | CHD1150 |
| A | ZN1300 |
| A | HOH1303 |
| A | HOH1313 |
| A | HOH1321 |
| A | HOH1445 |
| A | HOH1455 |
| A | HOH1480 |
| A | HOH1529 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CHD A 1150 |
| Chain | Residue |
| A | CYS46 |
| A | SER48 |
| A | LEU57 |
| A | HIS67 |
| A | PHE93 |
| A | SER116 |
| A | MET117 |
| A | CYS173 |
| A | VAL293 |
| A | ILE317 |
| A | NAD1100 |
| A | ZN1300 |
| A | HOH1365 |
| A | HOH1421 |
| A | HOH1476 |
| A | HOH1514 |
| A | HOH1521 |
| B | MET305 |
| B | LEU308 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 1200 |
| Chain | Residue |
| B | ARG47 |
| B | SER48 |
| B | HIS51 |
| B | CYS173 |
| B | THR177 |
| B | GLY198 |
| B | GLY200 |
| B | GLY201 |
| B | VAL202 |
| B | ASP222 |
| B | ILE223 |
| B | VAL267 |
| B | ILE268 |
| B | ARG270 |
| B | VAL291 |
| B | GLY292 |
| B | VAL293 |
| B | ALA316 |
| B | ILE317 |
| B | PHE318 |
| B | ARG368 |
| B | CHD1250 |
| B | ZN1302 |
| B | HOH1304 |
| B | HOH1326 |
| B | HOH1355 |
| B | HOH1427 |
| B | HOH1594 |
| B | HOH1622 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CHD B 1250 |
| Chain | Residue |
| A | LEU308 |
| B | CYS46 |
| B | SER48 |
| B | LEU57 |
| B | HIS67 |
| B | PHE93 |
| B | SER116 |
| B | MET117 |
| B | CYS173 |
| B | VAL293 |
| B | ILE317 |
| B | NAD1200 |
| B | ZN1302 |
| B | HOH1342 |
| B | HOH1357 |
| B | HOH1449 |
| B | HOH1474 |
| B | HOH1498 |
| A | MET305 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesiGegV |
| Chain | Residue | Details |
| A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG47 | |
| A | PHE228 | |
| A | GLY292 | |
| A | THR369 | |
| B | ARG47 | |
| B | GLU68 | |
| B | GLY98 | |
| B | SER101 | |
| B | LYS104 | |
| B | LEU112 | |
| B | GLY174 | |
| A | GLU68 | |
| B | LEU199 | |
| B | ILE223 | |
| B | PHE228 | |
| B | GLY292 | |
| B | THR369 | |
| A | GLY98 | |
| A | SER101 | |
| A | LYS104 | |
| A | LEU112 | |
| A | GLY174 | |
| A | LEU199 | |
| A | ILE223 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:5466062 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | LEU57 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | LEU57 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | SER48 | |
| A | HIS51 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | SER48 | |
| B | HIS51 |
