5MZ5
Crystal structure of aldehyde dehydrogenase 21 (ALDH21) from Physcomitrella patens in its apoform
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| A | 0008911 | molecular_function | lactaldehyde 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| B | 0008911 | molecular_function | lactaldehyde 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| C | 0008911 | molecular_function | lactaldehyde 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| D | 0008911 | molecular_function | lactaldehyde 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | ARG121 |
| A | PHE172 |
| A | ASN175 |
| A | ARG457 |
| A | TYR463 |
| A | HOH630 |
| A | HOH647 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ARG313 |
| A | LYS431 |
| A | HOH711 |
| A | ASP278 |
| A | TYR279 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLU132 |
| A | ARG135 |
| A | LYS477 |
| A | MET480 |
| A | ASP481 |
| A | LEU484 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLY249 |
| A | PRO250 |
| A | TRP253 |
| A | ASP468 |
| D | LYS58 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | LYS263 |
| A | VAL264 |
| B | LYS263 |
| B | VAL264 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 506 |
| Chain | Residue |
| A | LYS431 |
| A | ASP432 |
| D | LYS431 |
| D | ASP432 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ASN493 |
| A | THR496 |
| A | LEU497 |
| B | PRO281 |
| C | ASN434 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | ASP278 |
| B | TYR279 |
| B | ARG313 |
| B | LYS431 |
| B | HOH783 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ARG121 |
| B | PHE172 |
| B | ASN175 |
| B | TYR296 |
| B | ARG457 |
| B | TYR463 |
| B | HOH644 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLU132 |
| B | ARG135 |
| B | ILE136 |
| B | LYS477 |
| B | MET480 |
| B | ASP481 |
| B | HOH740 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | ALA324 |
| B | LYS327 |
| B | HOH642 |
| B | HOH645 |
| C | LEU367 |
| C | ASN372 |
| C | HOH630 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | TYR22 |
| B | ASN23 |
| B | PHE25 |
| B | GLU208 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | TRP170 |
| B | GLN300 |
| B | ALA349 |
| B | PHE398 |
| B | HOH789 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | ASP432 |
| B | ASN434 |
| C | LYS431 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 508 |
| Chain | Residue |
| B | ASP432 |
| C | ASP432 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 501 |
| Chain | Residue |
| C | GLU132 |
| C | ARG135 |
| C | ILE136 |
| C | LYS477 |
| C | MET480 |
| C | ASP481 |
| C | HOH624 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | ASP278 |
| C | TYR279 |
| C | LYS431 |
| C | HOH655 |
| C | HOH742 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| C | ARG121 |
| C | ASN175 |
| C | LEU176 |
| C | TYR296 |
| C | ARG457 |
| C | TYR463 |
| C | HOH701 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | ASP432 |
| C | ASN434 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 505 |
| Chain | Residue |
| C | GLU139 |
| C | TYR137 |
| C | GLY138 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 501 |
| Chain | Residue |
| C | LYS263 |
| C | VAL264 |
| C | ILE471 |
| D | LYS263 |
| D | VAL264 |
| D | ILE471 |
| site_id | AE4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 502 |
| Chain | Residue |
| D | ARG121 |
| D | PHE172 |
| D | ASN175 |
| D | LEU176 |
| D | TYR296 |
| D | ARG457 |
| D | TYR463 |
| D | HOH640 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | GLU132 |
| D | ARG135 |
| D | LYS477 |
| D | MET480 |
| D | ASP481 |
| D | HOH693 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 504 |
| Chain | Residue |
| D | ASP278 |
| D | TYR279 |
| D | LYS431 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGNAP |
| Chain | Residue | Details |
| A | MET266-PRO273 |
