4PZ2
Structure of Zm ALDH2-6 (RF2F) in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 601 |
| Chain | Residue |
| A | THR55 |
| A | ARG56 |
| A | ASP124 |
| A | GLN211 |
| A | HOH716 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 602 |
| Chain | Residue |
| A | SER49 |
| A | GLY50 |
| A | THR52 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 603 |
| Chain | Residue |
| A | ILE181 |
| A | PRO182 |
| A | TRP183 |
| A | ASN184 |
| A | MET189 |
| A | LYS207 |
| A | ALA209 |
| A | GLU210 |
| A | GLY240 |
| A | GLY244 |
| A | ALA245 |
| A | PHE258 |
| A | THR259 |
| A | GLY260 |
| A | SER261 |
| A | VAL264 |
| A | LEU267 |
| A | ILE268 |
| A | GLU283 |
| A | LEU284 |
| A | GLY285 |
| A | CYS317 |
| A | GLU417 |
| A | PHE419 |
| A | LEU445 |
| A | PHE483 |
| A | HOH710 |
| A | ILE180 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 604 |
| Chain | Residue |
| A | MET477 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 605 |
| Chain | Residue |
| A | GLN326 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 606 |
| Chain | Residue |
| A | GLN166 |
| A | HOH725 |
| C | ASN458 |
| D | GLN166 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 601 |
| Chain | Residue |
| B | THR55 |
| B | ARG56 |
| B | ASP124 |
| B | GLN211 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 602 |
| Chain | Residue |
| B | ILE180 |
| B | ILE181 |
| B | PRO182 |
| B | TRP183 |
| B | ASN184 |
| B | MET189 |
| B | LYS207 |
| B | ALA209 |
| B | GLU210 |
| B | GLY240 |
| B | GLY244 |
| B | ALA245 |
| B | PHE258 |
| B | THR259 |
| B | GLY260 |
| B | SER261 |
| B | VAL264 |
| B | LEU267 |
| B | ILE268 |
| B | GLU283 |
| B | LEU284 |
| B | GLY285 |
| B | CYS317 |
| B | GLU417 |
| B | PHE419 |
| B | PHE483 |
| B | HOH704 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 601 |
| Chain | Residue |
| C | THR55 |
| C | ARG56 |
| C | ASP124 |
| C | GLN211 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 602 |
| Chain | Residue |
| C | PHE483 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 603 |
| Chain | Residue |
| C | PHE293 |
| C | GLN326 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 605 |
| Chain | Residue |
| C | GLN365 |
| C | NAD606 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 606 |
| Chain | Residue |
| C | LEU267 |
| C | ILE268 |
| C | GLU283 |
| C | LEU284 |
| C | GLY285 |
| C | CYS317 |
| C | GLU417 |
| C | PHE419 |
| C | LEU445 |
| C | PHE483 |
| C | EDO605 |
| C | HOH717 |
| C | ILE180 |
| C | ILE181 |
| C | PRO182 |
| C | TRP183 |
| C | ASN184 |
| C | MET189 |
| C | LYS207 |
| C | ALA209 |
| C | GLU210 |
| C | GLY240 |
| C | GLY244 |
| C | ALA245 |
| C | PHE258 |
| C | THR259 |
| C | GLY260 |
| C | SER261 |
| C | VAL264 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 601 |
| Chain | Residue |
| D | THR55 |
| D | ARG56 |
| D | ASP124 |
| D | GLN211 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 602 |
| Chain | Residue |
| D | GLY100 |
| D | ALA104 |
| site_id | BC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD D 603 |
| Chain | Residue |
| D | ILE180 |
| D | ILE181 |
| D | PRO182 |
| D | TRP183 |
| D | ASN184 |
| D | MET189 |
| D | LYS207 |
| D | ALA209 |
| D | GLU210 |
| D | GLY240 |
| D | GLY244 |
| D | ALA245 |
| D | PHE258 |
| D | THR259 |
| D | GLY260 |
| D | SER261 |
| D | VAL264 |
| D | LEU267 |
| D | ILE268 |
| D | GLU283 |
| D | LEU284 |
| D | GLY285 |
| D | CYS317 |
| D | GLU417 |
| D | PHE419 |
| D | PHE483 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNKGEACVAAS |
| Chain | Residue | Details |
| A | PHE310-SER321 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU282-PRO289 |
