4H7N
The Structure of Putative Aldehyde Dehydrogenase PutA from Anabaena variabilis.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | GLN42 |
| A | GLY45 |
| A | ARG49 |
| A | LEU121 |
| A | PRO123 |
| A | ALA150 |
| A | HOH735 |
| A | HOH825 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | ALA226 |
| A | GLY438 |
| A | ARG449 |
| A | HOH673 |
| A | HOH876 |
| A | PHE202 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | ASN198 |
| A | ASP201 |
| A | ARG222 |
| A | HOH921 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | ARG213 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 501 |
| Chain | Residue |
| B | GLY190 |
| B | GLY193 |
| B | ALA194 |
| B | HOH749 |
| B | HOH879 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| B | GLY207 |
| B | GLN310 |
| B | HOH647 |
| B | HOH744 |
| B | HOH834 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | PHE135 |
| B | THR138 |
| B | SER262 |
| B | LEU264 |
| B | ALA422 |
| B | HOH885 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 501 |
| Chain | Residue |
| B | ASN433 |
| B | PHE434 |
| C | ARG222 |
| C | PHE223 |
| C | HOH690 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 502 |
| Chain | Residue |
| C | GLY190 |
| C | GLY193 |
| C | ALA194 |
| C | THR211 |
| C | HOH761 |
| C | HOH956 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 503 |
| Chain | Residue |
| C | LYS324 |
| C | ASN350 |
| C | ASN352 |
| C | HOH831 |
| C | HOH893 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 504 |
| Chain | Residue |
| C | PRO132 |
| C | GLY207 |
| C | GLN310 |
| C | HOH604 |
| C | HOH898 |
| C | HOH904 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 505 |
| Chain | Residue |
| B | ARG222 |
| B | ILE224 |
| B | HOH625 |
| B | HOH725 |
| C | ASN433 |
| C | PHE434 |
| C | HOH657 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 501 |
| Chain | Residue |
| D | GLY190 |
| D | GLY193 |
| D | ALA194 |
| D | THR211 |
| D | GLU214 |
| D | HOH769 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 502 |
| Chain | Residue |
| D | GLY207 |
| D | GLN310 |
| D | HOH617 |
| D | HOH717 |
| D | HOH736 |
| D | HOH757 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 503 |
| Chain | Residue |
| D | VAL200 |
| D | ARG222 |
| D | HOH820 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKDP |
| Chain | Residue | Details |
| A | LEU228-PRO235 |
