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 | 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 | 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 | 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 | 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 |