1U3W
Crystal Structure of Human Alcohol Dehydrogenase Gamma-2-Gamma-2 Isoform Complexed with N-1-Methylheptylformamide Determined to 1.45 Angstrom Resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005929 | cellular_component | cilium |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0035869 | cellular_component | ciliary transition zone |
| A | 0036064 | cellular_component | ciliary basal body |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042573 | biological_process | retinoic acid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) activity |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005929 | cellular_component | cilium |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0035869 | cellular_component | ciliary transition zone |
| B | 0036064 | cellular_component | ciliary basal body |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042573 | biological_process | retinoic acid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0120542 | molecular_function | ethanol dehydrogenase (NAD+) 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 376 |
| Chain | Residue |
| A | CYS46 |
| A | HIS67 |
| A | CYS174 |
| A | NAD1377 |
| A | FXY1378 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 375 |
| Chain | Residue |
| B | CYS97 |
| B | CYS100 |
| B | CYS103 |
| B | CYS111 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 376 |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS174 |
| B | NAD2377 |
| B | FXY2378 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A 1377 |
| Chain | Residue |
| A | ARG47 |
| A | SER48 |
| A | HIS51 |
| A | CYS174 |
| A | THR178 |
| A | GLY199 |
| A | GLY201 |
| A | GLY202 |
| A | VAL203 |
| A | ASP223 |
| A | ILE224 |
| A | LYS228 |
| A | VAL268 |
| A | ILE269 |
| A | GLN271 |
| A | THR274 |
| A | VAL292 |
| A | GLY293 |
| A | VAL294 |
| A | ALA317 |
| A | ILE318 |
| A | PHE319 |
| A | LEU362 |
| A | ARG369 |
| A | ZN376 |
| A | FXY1378 |
| A | HOH1379 |
| A | HOH1389 |
| A | HOH1406 |
| A | HOH1464 |
| A | HOH1487 |
| A | HOH1731 |
| A | HOH1818 |
| site_id | AC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD B 2377 |
| Chain | Residue |
| B | ARG47 |
| B | SER48 |
| B | HIS51 |
| B | CYS174 |
| B | THR178 |
| B | GLY199 |
| B | GLY201 |
| B | GLY202 |
| B | VAL203 |
| B | ASP223 |
| B | ILE224 |
| B | LYS228 |
| B | VAL268 |
| B | ILE269 |
| B | GLN271 |
| B | VAL292 |
| B | GLY293 |
| B | VAL294 |
| B | ALA317 |
| B | ILE318 |
| B | PHE319 |
| B | LEU362 |
| B | ARG369 |
| B | ZN376 |
| B | FXY2378 |
| B | HOH2379 |
| B | HOH2390 |
| B | HOH2416 |
| B | HOH2440 |
| B | HOH2497 |
| B | HOH2531 |
| B | HOH2618 |
| B | HOH2659 |
| B | HOH2679 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FXY A 1378 |
| Chain | Residue |
| A | CYS46 |
| A | SER48 |
| A | HIS67 |
| A | PHE93 |
| A | CYS174 |
| A | ZN376 |
| A | NAD1377 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FXY B 2378 |
| Chain | Residue |
| B | NAD2377 |
| A | MET306 |
| B | CYS46 |
| B | SER48 |
| B | HIS67 |
| B | PHE93 |
| B | CYS174 |
| B | ZN376 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesvGegV |
| Chain | Residue | Details |
| A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 38 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11274460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15449945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U3W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1HT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U3W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6391921","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00325","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
