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 | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
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 | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] 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 | 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 | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] 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 | 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 | 26 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0, ECO:0007744|PDB:1U3W |
Chain | Residue | Details |
A | ARG47 | |
A | PHE229 | |
A | GLY293 | |
A | ILE318 | |
A | THR370 | |
B | ARG47 | |
B | GLU68 | |
B | GLY98 | |
B | ARG101 | |
B | LYS104 | |
B | LEU112 | |
A | GLU68 | |
B | GLY175 | |
B | LEU200 | |
B | ILE224 | |
B | PHE229 | |
B | GLY293 | |
B | ILE318 | |
B | THR370 | |
A | GLY98 | |
A | ARG101 | |
A | LYS104 | |
A | LEU112 | |
A | GLY175 | |
A | LEU200 | |
A | ILE224 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:1HT0, ECO:0007744|PDB:1U3W |
Chain | Residue | Details |
A | GLY270 | |
B | GLY270 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:6391921 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00325 |
Chain | Residue | Details |
A | ILE23 | |
B | ILE23 |
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 |