7ADH
THREE-DIMENSIONAL STRUCTURE OF ISONICOTINIMIDYLATED LIVER ALCOHOL DEHYDROGENASE
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 375 |
Chain | Residue |
A | CYS46 |
A | SER48 |
A | HIS67 |
A | CYS174 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ZN A 376 |
Chain | Residue |
A | PHE319 |
A | PHE322 |
A | LYS323 |
A | SER324 |
A | CYS97 |
A | CYS100 |
A | CYS103 |
A | ASN109 |
A | CYS111 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NTN A 377 |
Chain | Residue |
A | LYS5 |
A | VAL41 |
A | ALA42 |
A | ALA70 |
A | LEU166 |
A | GLU167 |
A | LYS168 |
A | CYS170 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NTN A 378 |
Chain | Residue |
A | LYS8 |
A | VAL28 |
A | ALA29 |
A | ARG37 |
A | ILE38 |
A | ARG129 |
A | TYR149 |
A | THR150 |
A | VAL151 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NTN A 379 |
Chain | Residue |
A | LYS10 |
A | VAL13 |
A | TRP15 |
A | SER22 |
A | GLU24 |
A | GLU25 |
A | VAL26 |
A | THR131 |
A | CYS132 |
A | ILE137 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NTN A 380 |
Chain | Residue |
A | LYS18 |
A | SER54 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NTN A 381 |
Chain | Residue |
A | LYS19 |
A | NTN387 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NTN A 382 |
Chain | Residue |
A | LYS32 |
A | LEU279 |
A | CYS282 |
A | GLY287 |
A | VAL288 |
A | SER289 |
A | ARG312 |
A | THR313 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NTN A 383 |
Chain | Residue |
A | THR2 |
A | ALA3 |
A | GLY4 |
A | LYS5 |
A | VAL6 |
A | ILE7 |
A | PRO30 |
A | ARG37 |
A | LYS39 |
A | GLU74 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NTN A 384 |
Chain | Residue |
A | LYS88 |
A | ALA163 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NTN A 385 |
Chain | Residue |
A | ILE90 |
A | LYS99 |
A | ILE172 |
A | PHE176 |
A | SER177 |
A | VAL328 |
A | LEU331 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NTN A 386 |
Chain | Residue |
A | LYS113 |
A | GLN124 |
A | SER177 |
A | THR178 |
A | GLY179 |
A | GLY181 |
A | SER182 |
A | VAL186 |
A | ALA317 |
A | PHE319 |
A | GLY320 |
A | GLY321 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NTN A 387 |
Chain | Residue |
A | LYS135 |
A | NTN381 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NTN A 388 |
Chain | Residue |
A | ASP87 |
A | LYS159 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NTN A 389 |
Chain | Residue |
A | LYS168 |
A | ILE346 |
A | VAL349 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NTN A 390 |
Chain | Residue |
A | LYS185 |
A | NTN397 |
A | NTN398 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NTN A 391 |
Chain | Residue |
A | VAL80 |
A | LYS188 |
A | LYS315 |
A | LYS32 |
A | ALA33 |
A | HIS34 |
A | GLU35 |
A | VAL36 |
A | GLU78 |
site_id | BC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NTN A 392 |
Chain | Residue |
A | LYS212 |
site_id | CC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NTN A 393 |
Chain | Residue |
A | LYS226 |
site_id | CC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NTN A 394 |
Chain | Residue |
A | LYS228 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NTN A 395 |
Chain | Residue |
A | LYS228 |
A | LYS231 |
A | GLU366 |
A | ILE368 |
site_id | CC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NTN A 396 |
Chain | Residue |
A | LYS247 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NTN A 397 |
Chain | Residue |
A | THR82 |
A | PRO106 |
A | LYS185 |
A | LYS325 |
A | NTN390 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NTN A 398 |
Chain | Residue |
A | GLY98 |
A | ASP326 |
A | LYS330 |
A | NTN390 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NTN A 399 |
Chain | Residue |
A | MET306 |
A | LYS354 |
A | GLU357 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06525 |
Chain | Residue | Details |
A | ASP49 | |
A | GLY293 | |
A | GLY320 |
Chain | Residue | Details |
A | GLY98 | |
A | ARG101 | |
A | LYS104 | |
A | LEU112 |
Chain | Residue | Details |
A | GLY175 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
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 |
Chain | Residue | Details |
A | ILE224 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:5466062 |
Chain | Residue | Details |
A | 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 | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
A | SER48 | |
A | 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 |