1LDE
HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINE
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 | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
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 | 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 | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
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 |
C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
C | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
C | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0042572 | biological_process | retinol metabolic process |
C | 0042573 | biological_process | retinoic acid metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
D | 0004024 | molecular_function | alcohol dehydrogenase (NAD+) activity, zinc-dependent |
D | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0042572 | biological_process | retinol metabolic process |
D | 0042573 | biological_process | retinoic acid metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 375 |
Chain | Residue |
A | CYS46 |
A | HIS67 |
A | CYS174 |
A | NAD377 |
A | FPI378 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 376 |
Chain | Residue |
A | CYS97 |
A | CYS100 |
A | CYS103 |
A | CYS111 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 375 |
Chain | Residue |
B | CYS46 |
B | SER48 |
B | HIS67 |
B | CYS174 |
B | NAD377 |
B | FPI378 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 376 |
Chain | Residue |
B | CYS97 |
B | CYS100 |
B | CYS103 |
B | CYS111 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 375 |
Chain | Residue |
C | CYS46 |
C | HIS67 |
C | CYS174 |
C | NAD377 |
C | FPI378 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 376 |
Chain | Residue |
C | CYS97 |
C | CYS100 |
C | CYS103 |
C | CYS111 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 375 |
Chain | Residue |
D | CYS46 |
D | HIS67 |
D | CYS174 |
D | NAD377 |
D | FPI378 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 376 |
Chain | Residue |
D | CYS97 |
D | CYS100 |
D | CYS103 |
D | CYS111 |
site_id | AC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 377 |
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 | ARG271 |
A | VAL292 |
A | GLY293 |
A | VAL294 |
A | ALA317 |
A | ILE318 |
A | PHE319 |
A | ARG369 |
A | ZN375 |
A | FPI378 |
A | HOH402 |
A | HOH415 |
A | HOH416 |
A | HOH518 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FPI A 378 |
Chain | Residue |
A | CYS46 |
A | SER48 |
A | HIS67 |
A | LEU116 |
A | LEU141 |
A | CYS174 |
A | VAL294 |
A | ZN375 |
A | NAD377 |
site_id | BC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 377 |
Chain | Residue |
B | ARG369 |
B | ZN375 |
B | FPI378 |
B | HOH413 |
B | HOH414 |
B | HOH513 |
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 | ARG271 |
B | VAL292 |
B | GLY293 |
B | VAL294 |
B | ALA317 |
B | ILE318 |
B | PHE319 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FPI B 378 |
Chain | Residue |
B | CYS46 |
B | SER48 |
B | HIS67 |
B | LEU116 |
B | LEU141 |
B | CYS174 |
B | VAL294 |
B | ZN375 |
B | NAD377 |
site_id | BC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD C 377 |
Chain | Residue |
C | ARG47 |
C | SER48 |
C | HIS51 |
C | CYS174 |
C | THR178 |
C | GLY199 |
C | LEU200 |
C | GLY201 |
C | GLY202 |
C | VAL203 |
C | ASP223 |
C | ILE224 |
C | LYS228 |
C | VAL268 |
C | ILE269 |
C | ARG271 |
C | VAL292 |
C | GLY293 |
C | VAL294 |
C | ALA317 |
C | ILE318 |
C | PHE319 |
C | ARG369 |
C | ZN375 |
C | FPI378 |
C | HOH406 |
C | HOH409 |
C | HOH421 |
C | HOH422 |
C | HOH483 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FPI C 378 |
Chain | Residue |
C | CYS46 |
C | SER48 |
C | HIS67 |
C | LEU116 |
C | LEU141 |
C | CYS174 |
C | VAL294 |
C | ZN375 |
C | NAD377 |
site_id | BC6 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD D 377 |
Chain | Residue |
D | ARG47 |
D | SER48 |
D | HIS51 |
D | CYS174 |
D | THR178 |
D | GLY201 |
D | GLY202 |
D | VAL203 |
D | ASP223 |
D | ILE224 |
D | LYS228 |
D | VAL268 |
D | ILE269 |
D | ARG271 |
D | VAL292 |
D | GLY293 |
D | VAL294 |
D | ALA317 |
D | ILE318 |
D | PHE319 |
D | ARG369 |
D | ZN375 |
D | FPI378 |
D | HOH447 |
D | HOH451 |
D | HOH464 |
D | HOH532 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FPI D 378 |
Chain | Residue |
D | CYS46 |
D | SER48 |
D | HIS67 |
D | LEU116 |
D | LEU141 |
D | CYS174 |
D | ZN375 |
D | NAD377 |
site_id | NAD |
Number of Residues | 4 |
Details | NICOTINAMIDE-ADENINE-DINUCLEOTIDE SITE |
Chain | Residue |
A | ARG47 |
A | SER48 |
A | HIS51 |
A | THR178 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesiGegV |
Chain | Residue | Details |
A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG47 | |
A | GLU68 | |
B | ARG47 | |
B | GLU68 | |
C | ARG47 | |
C | GLU68 | |
D | ARG47 | |
D | GLU68 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06525 |
Chain | Residue | Details |
A | ASP49 | |
D | ASP49 | |
D | GLY293 | |
D | GLY320 | |
A | GLY293 | |
A | GLY320 | |
B | ASP49 | |
B | GLY293 | |
B | GLY320 | |
C | ASP49 | |
C | GLY293 | |
C | GLY320 |
Chain | Residue | Details |
A | GLY98 | |
C | ARG101 | |
C | LYS104 | |
C | LEU112 | |
D | GLY98 | |
D | ARG101 | |
D | LYS104 | |
D | LEU112 | |
A | ARG101 | |
A | LYS104 | |
A | LEU112 | |
B | GLY98 | |
B | ARG101 | |
B | LYS104 | |
B | LEU112 | |
C | GLY98 |
Chain | Residue | Details |
A | GLY175 | |
B | GLY175 | |
C | GLY175 | |
D | GLY175 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH |
Chain | Residue | Details |
A | LEU200 | |
B | LEU200 | |
C | LEU200 | |
D | LEU200 |
Chain | Residue | Details |
A | ILE224 | |
B | ILE224 | |
C | ILE224 | |
D | ILE224 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1JU9, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1QLH, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:5ADH, ECO:0007744|PDB:6ADH |
Chain | Residue | Details |
A | PHE229 | |
B | PHE229 | |
C | PHE229 | |
D | PHE229 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15299346, ECO:0007744|PDB:1A71, ECO:0007744|PDB:1ADB, ECO:0007744|PDB:1AXE, ECO:0007744|PDB:1AXG, ECO:0007744|PDB:1BTO, ECO:0007744|PDB:1HET, ECO:0007744|PDB:1HEU, ECO:0007744|PDB:1HF3, ECO:0007744|PDB:1HLD, ECO:0007744|PDB:1LDE, ECO:0007744|PDB:1LDY, ECO:0007744|PDB:1MG0, ECO:0007744|PDB:1MGO, ECO:0007744|PDB:1N8K, ECO:0007744|PDB:1N92, ECO:0007744|PDB:1P1R, ECO:0007744|PDB:1QV6, ECO:0007744|PDB:1QV7, ECO:0007744|PDB:2JHF, ECO:0007744|PDB:2JHG, ECO:0007744|PDB:2OHX, ECO:0007744|PDB:2OXI, ECO:0007744|PDB:3BTO, ECO:0007744|PDB:3OQ6, ECO:0007744|PDB:4DWV, ECO:0007744|PDB:4DXH, ECO:0007744|PDB:4NFH, ECO:0007744|PDB:4NFS, ECO:0007744|PDB:4NG5, ECO:0007744|PDB:4XD2, ECO:0007744|PDB:6ADH |
Chain | Residue | Details |
A | THR370 | |
B | THR370 | |
C | THR370 | |
D | THR370 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:5466062 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 | |
C | THR2 | |
D | THR2 |
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 | 1 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
C | LEU57 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
D | LEU57 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
A | SER48 | |
A | HIS51 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
B | SER48 | |
B | HIS51 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
C | SER48 | |
C | HIS51 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
D | SER48 | |
D | HIS51 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 256 |
Chain | Residue | Details |
A | ARG47 | metal ligand |
A | ASP49 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | VAL52 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | GLU68 | metal ligand |
A | GLY175 | metal ligand |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 256 |
Chain | Residue | Details |
B | ARG47 | metal ligand |
B | ASP49 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | VAL52 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | GLU68 | metal ligand |
B | GLY175 | metal ligand |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 256 |
Chain | Residue | Details |
C | ARG47 | metal ligand |
C | ASP49 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | VAL52 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | GLU68 | metal ligand |
C | GLY175 | metal ligand |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 256 |
Chain | Residue | Details |
D | ARG47 | metal ligand |
D | ASP49 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | VAL52 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | GLU68 | metal ligand |
D | GLY175 | metal ligand |