1HDY
THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES
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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 376 |
Chain | Residue |
A | CYS46 |
A | HIS67 |
A | CYS174 |
A | NAD377 |
A | PYZ378 |
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 | NAD377 |
B | PYZ378 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 601 |
Chain | Residue |
B | ARG128 |
site_id | AC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 377 |
Chain | Residue |
A | CYS46 |
A | HIS47 |
A | THR48 |
A | HIS51 |
A | CYS174 |
A | THR178 |
A | GLY201 |
A | GLY202 |
A | VAL203 |
A | ASP223 |
A | ILE224 |
A | LYS228 |
A | VAL268 |
A | ILE269 |
A | ARG271 |
A | VAL292 |
A | VAL294 |
A | ALA317 |
A | TYR319 |
A | LEU362 |
A | ARG369 |
A | ZN376 |
A | PYZ378 |
A | HOH382 |
A | HOH383 |
A | HOH384 |
A | HOH385 |
B | LEU309 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYZ A 378 |
Chain | Residue |
A | CYS46 |
A | THR48 |
A | HIS67 |
A | PHE93 |
A | CYS174 |
A | ZN376 |
A | NAD377 |
site_id | AC8 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD B 377 |
Chain | Residue |
B | ZN376 |
B | PYZ378 |
B | HOH605 |
B | CYS46 |
B | HIS47 |
B | THR48 |
B | HIS51 |
B | CYS174 |
B | THR178 |
B | GLY199 |
B | LEU200 |
B | GLY201 |
B | GLY202 |
B | VAL203 |
B | ASP223 |
B | ILE224 |
B | LYS228 |
B | VAL268 |
B | ILE269 |
B | ARG271 |
B | VAL292 |
B | GLY293 |
B | VAL294 |
B | ALA317 |
B | TYR319 |
B | ARG369 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYZ B 378 |
Chain | Residue |
B | CYS46 |
B | THR48 |
B | HIS67 |
B | PHE93 |
B | CYS174 |
B | ZN376 |
B | NAD377 |
site_id | CAX |
Number of Residues | 1 |
Details |
Chain | Residue |
A | PYZ378 |
site_id | CBX |
Number of Residues | 1 |
Details |
Chain | Residue |
B | PYZ378 |
site_id | NAD |
Number of Residues | 1 |
Details |
Chain | Residue |
A | NAD377 |
site_id | NBD |
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 | CYS103 | |
A | CYS111 | |
A | CYS174 | |
A | GLY199 | |
A | ASP223 | |
A | LYS228 | |
A | VAL292 | |
A | ARG369 | |
B | CYS46 | |
B | HIS67 | |
B | CYS97 | |
B | CYS100 | |
B | CYS103 | |
B | CYS111 | |
B | CYS174 | |
B | GLY199 | |
B | ASP223 | |
B | LYS228 | |
B | VAL292 | |
B | ARG369 | |
A | CYS97 | |
A | CYS46 | |
A | HIS67 | |
A | CYS100 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:6391920 |
Chain | Residue | Details |
A | SER1 | |
B | SER1 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER22 | |
B | SER22 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | TYR34 | |
B | TYR34 |