1AGN
X-RAY STRUCTURE OF HUMAN SIGMA ALCOHOL DEHYDROGENASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| A | 0004031 | molecular_function | aldehyde oxidase activity |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009617 | biological_process | response to bacterium |
| A | 0010430 | biological_process | fatty acid omega-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019841 | molecular_function | retinol binding |
| A | 0035276 | molecular_function | ethanol binding |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042573 | biological_process | retinoic acid metabolic process |
| A | 0045471 | biological_process | response to ethanol |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048019 | molecular_function | receptor antagonist activity |
| A | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
| B | 0001523 | biological_process | retinoid metabolic process |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| B | 0004031 | molecular_function | aldehyde oxidase activity |
| B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009617 | biological_process | response to bacterium |
| B | 0010430 | biological_process | fatty acid omega-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019841 | molecular_function | retinol binding |
| B | 0035276 | molecular_function | ethanol binding |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042573 | biological_process | retinoic acid metabolic process |
| B | 0045471 | biological_process | response to ethanol |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048019 | molecular_function | receptor antagonist activity |
| B | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
| C | 0001523 | biological_process | retinoid metabolic process |
| C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| C | 0004031 | molecular_function | aldehyde oxidase activity |
| C | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009617 | biological_process | response to bacterium |
| C | 0010430 | biological_process | fatty acid omega-oxidation |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019841 | molecular_function | retinol binding |
| C | 0035276 | molecular_function | ethanol binding |
| C | 0042572 | biological_process | retinol metabolic process |
| C | 0042573 | biological_process | retinoic acid metabolic process |
| C | 0045471 | biological_process | response to ethanol |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048019 | molecular_function | receptor antagonist activity |
| C | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
| D | 0001523 | biological_process | retinoid metabolic process |
| D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
| D | 0004031 | molecular_function | aldehyde oxidase activity |
| D | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009617 | biological_process | response to bacterium |
| D | 0010430 | biological_process | fatty acid omega-oxidation |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019841 | molecular_function | retinol binding |
| D | 0035276 | molecular_function | ethanol binding |
| D | 0042572 | biological_process | retinol metabolic process |
| D | 0042573 | biological_process | retinoic acid metabolic process |
| D | 0045471 | biological_process | response to ethanol |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048019 | molecular_function | receptor antagonist activity |
| D | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 375 |
| Chain | Residue |
| A | CYS97 |
| A | CYS100 |
| A | CYS103 |
| A | CYS111 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 376 |
| Chain | Residue |
| A | CYS46 |
| A | THR48 |
| A | HIS67 |
| A | CYS174 |
| A | NAD377 |
| A | ACT378 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS271 |
| A | NAD377 |
| A | ACT501 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 378 |
| Chain | Residue |
| A | THR48 |
| A | MET141 |
| A | ZN376 |
| A | NAD377 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 501 |
| Chain | Residue |
| A | HIS271 |
| A | NAD377 |
| A | ZN401 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 502 |
| Chain | Residue |
| A | GLU357 |
| A | GLU360 |
| C | PRO136 |
| C | HIS138 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 375 |
| Chain | Residue |
| B | CYS97 |
| B | CYS100 |
| B | CYS103 |
| B | CYS111 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 376 |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS174 |
| B | ACT378 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS271 |
| B | NAD377 |
| B | ACT501 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 403 |
| Chain | Residue |
| B | HIS138 |
| D | GLU357 |
| D | GLU360 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | ASP341 |
| B | ACT502 |
| B | ACT503 |
| D | GLU99 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 378 |
| Chain | Residue |
| B | CYS46 |
| B | THR48 |
| B | HIS67 |
| B | PHE93 |
| B | MET141 |
| B | CYS174 |
| B | ZN376 |
| B | NAD377 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 501 |
| Chain | Residue |
| B | HIS271 |
| B | NAD377 |
| B | ZN401 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 503 |
| Chain | Residue |
| B | ASP341 |
| B | ZN402 |
| D | LYS34 |
| D | GLU99 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 502 |
| Chain | Residue |
| D | GLU99 |
| B | ASP341 |
| B | ZN402 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 375 |
| Chain | Residue |
| C | CYS97 |
| C | CYS100 |
| C | CYS103 |
| C | CYS111 |
| C | ILE112 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 376 |
| Chain | Residue |
| C | CYS46 |
| C | THR48 |
| C | HIS67 |
| C | CYS174 |
| C | NAD377 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | HIS271 |
| C | NAD377 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 378 |
| Chain | Residue |
| C | PHE93 |
| C | VAL294 |
| C | NAD377 |
| D | PHE309 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 375 |
| Chain | Residue |
| D | CYS97 |
| D | CYS100 |
| D | CYS103 |
| D | CYS111 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 376 |
| Chain | Residue |
| D | CYS46 |
| D | THR48 |
| D | HIS67 |
| D | CYS174 |
| D | ACT378 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 401 |
| Chain | Residue |
| D | HIS271 |
| D | NAD377 |
| D | ACT501 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 402 |
| Chain | Residue |
| A | GLU25 |
| D | GLU252 |
| D | GLU256 |
| site_id | CC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN D 403 |
| Chain | Residue |
| D | HIS138 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT D 378 |
| Chain | Residue |
| D | THR48 |
| D | MET141 |
| D | VAL294 |
| D | ZN376 |
| D | NAD377 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 501 |
| Chain | Residue |
| D | HIS271 |
| D | NAD377 |
| D | ZN401 |
| site_id | CC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 377 |
| Chain | Residue |
| A | CYS46 |
| A | ARG47 |
| A | THR48 |
| A | HIS51 |
| A | CYS174 |
| A | THR178 |
| A | LEU200 |
| A | GLY201 |
| A | GLY202 |
| A | VAL203 |
| A | ASP223 |
| A | LEU224 |
| A | LYS228 |
| A | ILE269 |
| A | GLY270 |
| A | HIS271 |
| A | VAL292 |
| A | GLY293 |
| A | VAL294 |
| A | CYS317 |
| A | PHE319 |
| A | ARG369 |
| A | ZN376 |
| A | ACT378 |
| A | ZN401 |
| A | ACT501 |
| B | PHE309 |
| site_id | DC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B 377 |
| Chain | Residue |
| A | PHE309 |
| B | ARG47 |
| B | THR48 |
| B | HIS51 |
| B | CYS174 |
| B | THR178 |
| B | GLY199 |
| B | LEU200 |
| B | GLY201 |
| B | GLY202 |
| B | VAL203 |
| B | ASP223 |
| B | LYS228 |
| B | VAL268 |
| B | ILE269 |
| B | HIS271 |
| B | VAL292 |
| B | VAL294 |
| B | CYS317 |
| B | VAL318 |
| B | PHE319 |
| B | ARG369 |
| B | ACT378 |
| B | ZN401 |
| B | ACT501 |
| site_id | DC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD C 377 |
| Chain | Residue |
| C | ARG47 |
| C | THR48 |
| C | HIS51 |
| C | CYS174 |
| C | THR178 |
| C | LEU200 |
| C | GLY201 |
| C | GLY202 |
| C | VAL203 |
| C | ASP223 |
| C | ASN225 |
| C | LYS228 |
| C | ILE269 |
| C | VAL292 |
| C | GLY293 |
| C | VAL294 |
| C | CYS317 |
| C | PHE319 |
| C | ARG369 |
| C | ZN376 |
| C | ACT378 |
| C | ZN401 |
| D | PHE309 |
| site_id | DC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD D 377 |
| Chain | Residue |
| C | PHE309 |
| D | ARG47 |
| D | THR48 |
| D | HIS51 |
| D | THR178 |
| D | LEU200 |
| D | GLY201 |
| D | GLY202 |
| D | VAL203 |
| D | ASP223 |
| D | LEU224 |
| D | LYS228 |
| D | ILE269 |
| D | HIS271 |
| D | VAL292 |
| D | GLY293 |
| D | VAL294 |
| D | CYS317 |
| D | VAL318 |
| D | PHE319 |
| D | ARG369 |
| D | ACT378 |
| D | ZN401 |
| D | ACT501 |
| site_id | ZN1 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| A | CYS97 |
| A | CYS100 |
| A | CYS103 |
| A | CYS111 |
| A | ZN375 |
| site_id | ZN2 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| A | ACT378 |
| A | CYS46 |
| A | HIS67 |
| A | CYS174 |
| A | ZN376 |
| site_id | ZN3 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| B | CYS97 |
| B | CYS100 |
| B | CYS103 |
| B | CYS111 |
| B | ZN375 |
| site_id | ZN4 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS174 |
| B | ZN376 |
| B | ACT378 |
| site_id | ZN5 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| A | CYS97 |
| A | CYS100 |
| A | CYS103 |
| A | CYS111 |
| A | ZN375 |
| site_id | ZN6 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| A | CYS46 |
| A | HIS67 |
| A | CYS174 |
| A | ZN376 |
| A | ACT378 |
| site_id | ZN7 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| B | CYS97 |
| B | CYS100 |
| B | CYS103 |
| B | CYS111 |
| B | ZN375 |
| site_id | ZN8 |
| Number of Residues | 5 |
| Details | ZINC BINDING SITE |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS174 |
| B | ZN376 |
| B | ACT378 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaTGIvesiGegV |
| Chain | Residue | Details |
| A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10631979, ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, ECO:0007744|PDB:1D1T |
| Chain | Residue | Details |
| A | VAL58 | |
| A | VAL235 | |
| A | CYS240 | |
| A | SER281 | |
| A | ASP304 | |
| A | PRO329 | |
| B | VAL58 | |
| B | SER59 | |
| B | GLY79 | |
| B | ASN109 | |
| B | ILE112 | |
| A | SER59 | |
| B | ASP115 | |
| B | ALA124 | |
| B | THR186 | |
| B | CYS211 | |
| B | VAL235 | |
| B | CYS240 | |
| B | SER281 | |
| B | ASP304 | |
| B | PRO329 | |
| C | VAL58 | |
| A | GLY79 | |
| C | SER59 | |
| C | GLY79 | |
| C | ASN109 | |
| C | ILE112 | |
| C | ASP115 | |
| C | ALA124 | |
| C | THR186 | |
| C | CYS211 | |
| C | VAL235 | |
| C | CYS240 | |
| A | ASN109 | |
| C | SER281 | |
| C | ASP304 | |
| C | PRO329 | |
| D | VAL58 | |
| D | SER59 | |
| D | GLY79 | |
| D | ASN109 | |
| D | ILE112 | |
| D | ASP115 | |
| D | ALA124 | |
| A | ILE112 | |
| D | THR186 | |
| D | CYS211 | |
| D | VAL235 | |
| D | CYS240 | |
| D | SER281 | |
| D | ASP304 | |
| D | PRO329 | |
| A | ASP115 | |
| A | ALA124 | |
| A | THR186 | |
| A | CYS211 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | THR48 | |
| A | ARG47 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| B | MET57 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| C | MET57 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| D | MET57 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| B | THR48 | |
| B | ARG47 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| C | THR48 | |
| C | ARG47 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| D | THR48 | |
| D | ARG47 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | THR48 | |
| A | HIS51 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| B | THR48 | |
| B | HIS51 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| C | THR48 | |
| C | HIS51 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| D | THR48 | |
| D | HIS51 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | MET57 |
