2JG7
Crystal structure of Seabream Antiquitin and Elucidation of its substrate specificity
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| E | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD A1510 |
| Chain | Residue |
| A | ILE162 |
| A | GLY229 |
| A | THR230 |
| A | PHE243 |
| A | THR244 |
| A | GLY245 |
| A | SER246 |
| A | VAL249 |
| A | MET252 |
| A | VAL253 |
| A | GLU267 |
| A | THR163 |
| A | LEU268 |
| A | GLY269 |
| A | CYS301 |
| A | GLU398 |
| A | PHE400 |
| A | PHE467 |
| A | ALA164 |
| A | PHE165 |
| A | ASN166 |
| A | LYS189 |
| A | ALA191 |
| A | PRO192 |
| A | ALA226 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B1510 |
| Chain | Residue |
| B | ILE162 |
| B | THR163 |
| B | ALA164 |
| B | PHE165 |
| B | ASN166 |
| B | LYS189 |
| B | ALA191 |
| B | PRO192 |
| B | ALA226 |
| B | GLY229 |
| B | THR230 |
| B | PHE243 |
| B | THR244 |
| B | GLY245 |
| B | SER246 |
| B | VAL249 |
| B | MET252 |
| B | VAL253 |
| B | GLU267 |
| B | LEU268 |
| B | GLY269 |
| B | CYS301 |
| B | GLU398 |
| B | PHE400 |
| B | PHE467 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD C1510 |
| Chain | Residue |
| C | ILE162 |
| C | THR163 |
| C | ALA164 |
| C | PHE165 |
| C | ASN166 |
| C | LYS189 |
| C | ALA191 |
| C | PRO192 |
| C | ALA226 |
| C | GLY229 |
| C | THR230 |
| C | PHE243 |
| C | THR244 |
| C | GLY245 |
| C | SER246 |
| C | VAL249 |
| C | MET252 |
| C | VAL253 |
| C | GLU267 |
| C | LEU268 |
| C | GLY269 |
| C | CYS301 |
| C | GLU398 |
| C | PHE400 |
| C | PHE467 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD D1510 |
| Chain | Residue |
| D | PHE467 |
| D | ILE162 |
| D | THR163 |
| D | ALA164 |
| D | PHE165 |
| D | ASN166 |
| D | LYS189 |
| D | ALA191 |
| D | PRO192 |
| D | ALA226 |
| D | GLY229 |
| D | THR230 |
| D | PHE243 |
| D | THR244 |
| D | GLY245 |
| D | SER246 |
| D | VAL249 |
| D | MET252 |
| D | VAL253 |
| D | GLU267 |
| D | LEU268 |
| D | GLY269 |
| D | CYS301 |
| D | GLU398 |
| D | PHE400 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD E1510 |
| Chain | Residue |
| E | ILE162 |
| E | THR163 |
| E | ALA164 |
| E | PHE165 |
| E | ASN166 |
| E | LYS189 |
| E | ALA191 |
| E | PRO192 |
| E | ALA226 |
| E | GLY229 |
| E | THR230 |
| E | PHE243 |
| E | THR244 |
| E | GLY245 |
| E | SER246 |
| E | VAL249 |
| E | MET252 |
| E | VAL253 |
| E | GLU267 |
| E | LEU268 |
| E | GLY269 |
| E | CYS301 |
| E | GLU398 |
| E | PHE400 |
| E | PHE467 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD F1510 |
| Chain | Residue |
| F | ILE162 |
| F | THR163 |
| F | ALA164 |
| F | PHE165 |
| F | ASN166 |
| F | LYS189 |
| F | ALA191 |
| F | PRO192 |
| F | ALA226 |
| F | GLY229 |
| F | THR230 |
| F | PHE243 |
| F | THR244 |
| F | GLY245 |
| F | SER246 |
| F | VAL249 |
| F | MET252 |
| F | VAL253 |
| F | GLU267 |
| F | LEU268 |
| F | GLY269 |
| F | CYS301 |
| F | GLU398 |
| F | PHE400 |
| F | PHE467 |
| F | HOH2021 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD G1510 |
| Chain | Residue |
| G | ILE162 |
| G | THR163 |
| G | ALA164 |
| G | PHE165 |
| G | ASN166 |
| G | LYS189 |
| G | ALA191 |
| G | PRO192 |
| G | ALA226 |
| G | GLY229 |
| G | THR230 |
| G | PHE243 |
| G | THR244 |
| G | GLY245 |
| G | SER246 |
| G | VAL249 |
| G | MET252 |
| G | VAL253 |
| G | GLU267 |
| G | LEU268 |
| G | GLY269 |
| G | CYS301 |
| G | GLU398 |
| G | PHE400 |
| G | PHE467 |
| G | HOH2015 |
| G | HOH2030 |
| G | HOH2031 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD H1510 |
| Chain | Residue |
| H | ILE162 |
| H | THR163 |
| H | ALA164 |
| H | PHE165 |
| H | ASN166 |
| H | LYS189 |
| H | ALA191 |
| H | PRO192 |
| H | ALA226 |
| H | GLY229 |
| H | THR230 |
| H | PHE243 |
| H | THR244 |
| H | GLY245 |
| H | SER246 |
| H | VAL249 |
| H | MET252 |
| H | VAL253 |
| H | GLU267 |
| H | LEU268 |
| H | GLY269 |
| H | CYS301 |
| H | GLU398 |
| H | PHE400 |
| H | PHE467 |
| H | HOH2014 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNNA |
| Chain | Residue | Details |
| A | LEU266-ALA273 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | ASN166 | |
| A | CYS301 | |
| A | GLU267 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | ASN166 | |
| B | CYS301 | |
| B | GLU267 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | ASN166 | |
| C | CYS301 | |
| C | GLU267 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | ASN166 | |
| D | CYS301 | |
| D | GLU267 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| E | ASN166 | |
| E | CYS301 | |
| E | GLU267 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| F | ASN166 | |
| F | CYS301 | |
| F | GLU267 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| G | ASN166 | |
| G | CYS301 | |
| G | GLU267 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| H | ASN166 | |
| H | CYS301 | |
| H | GLU267 |
