3HUD
THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS
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 | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006066 | biological_process | alcohol metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| 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 | 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 | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006066 | biological_process | alcohol metabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| 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 | 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 376 |
| Chain | Residue |
| A | CYS46 |
| A | HIS67 |
| A | CYS174 |
| A | NAD377 |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 376 |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS174 |
| B | NAD377 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD A 377 |
| Chain | Residue |
| A | ARG47 |
| A | THR48 |
| A | HIS51 |
| A | CYS174 |
| A | THR178 |
| A | LEU200 |
| A | GLY201 |
| A | VAL203 |
| A | ASP223 |
| A | ILE224 |
| A | LYS228 |
| A | ILE269 |
| A | VAL292 |
| A | VAL294 |
| A | ALA317 |
| A | VAL318 |
| A | TYR319 |
| A | ARG369 |
| A | ZN376 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B 377 |
| Chain | Residue |
| B | ARG47 |
| B | THR48 |
| B | HIS51 |
| B | PHE93 |
| B | CYS174 |
| B | THR178 |
| B | GLY199 |
| B | LEU200 |
| B | GLY201 |
| B | GLY202 |
| B | VAL203 |
| B | ASP223 |
| B | LYS228 |
| B | ILE269 |
| B | ARG271 |
| B | VAL292 |
| B | GLY293 |
| B | VAL294 |
| B | ALA317 |
| B | VAL318 |
| B | TYR319 |
| B | ARG369 |
| B | ZN376 |
| site_id | ND1 |
| Number of Residues | 1 |
| Details |
| Chain | Residue |
| A | NAD377 |
| site_id | ND2 |
| Number of Residues | 1 |
| Details |
| Chain | Residue |
| B | NAD377 |
| site_id | ZA1 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| A | CYS46 |
| A | HIS67 |
| A | CYS174 |
| A | ZN376 |
| site_id | ZA2 |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| A | CYS97 |
| A | CYS100 |
| A | CYS103 |
| A | CYS111 |
| A | ZN375 |
| site_id | ZB1 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| B | CYS46 |
| B | HIS67 |
| B | CYS174 |
| B | ZN376 |
| site_id | ZB2 |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| B | CYS97 |
| B | CYS100 |
| B | CYS103 |
| B | CYS111 |
| B | ZN375 |
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 | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS104 | |
| A | LEU112 | |
| A | GLY175 | |
| A | LEU200 | |
| A | ILE224 | |
| A | PHE229 | |
| A | GLY293 | |
| A | THR370 | |
| B | ARG47 | |
| B | GLU68 | |
| B | GLY98 | |
| B | ARG101 | |
| B | LYS104 | |
| B | LEU112 | |
| B | GLY175 | |
| B | LEU200 | |
| B | ILE224 | |
| B | PHE229 | |
| B | GLY293 | |
| B | THR370 | |
| A | ARG47 | |
| A | GLU68 | |
| A | GLY98 | |
| A | ARG101 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:6391920 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | ILE23 | |
| B | ILE23 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | GLU35 | |
| B | GLU35 |
