5UCD
Benzaldehyde Dehydrogenase, a Class 3 Aldehyde Dehydrogenase, with bound NADP+ and Benzoate Adduct
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004028 | molecular_function | 3-chloroallyl aldehyde dehydrogenase activity |
A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006081 | biological_process | cellular aldehyde metabolic process |
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 | 0018477 | molecular_function | benzaldehyde dehydrogenase (NADP+) activity |
A | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
A | 0019596 | biological_process | mandelate catabolic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004028 | molecular_function | 3-chloroallyl aldehyde dehydrogenase activity |
B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006081 | biological_process | cellular aldehyde metabolic process |
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 | 0018477 | molecular_function | benzaldehyde dehydrogenase (NADP+) activity |
B | 0018479 | molecular_function | benzaldehyde dehydrogenase (NAD+) activity |
B | 0019596 | biological_process | mandelate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue NAP A 501 |
Chain | Residue |
A | ILE116 |
A | ASN178 |
A | THR192 |
A | GLY193 |
A | SER194 |
A | VAL197 |
A | GLU215 |
A | LEU216 |
A | GLY217 |
A | ZBZ249 |
A | GLU337 |
A | GLY117 |
A | PHE339 |
A | LEU366 |
A | PHE406 |
A | HOH616 |
A | HOH631 |
A | PRO118 |
A | PHE119 |
A | ASN120 |
A | LYS143 |
A | SER145 |
A | GLU146 |
A | ARG175 |
site_id | AC2 |
Number of Residues | 25 |
Details | binding site for residue NAP B 501 |
Chain | Residue |
B | ILE116 |
B | GLY117 |
B | PHE119 |
B | ASN120 |
B | LEU125 |
B | LYS143 |
B | SER145 |
B | GLU146 |
B | THR147 |
B | ARG175 |
B | ASN178 |
B | PHE191 |
B | THR192 |
B | GLY193 |
B | SER194 |
B | VAL197 |
B | GLU215 |
B | LEU216 |
B | GLY217 |
B | ZBZ249 |
B | GLU337 |
B | PHE339 |
B | LEU366 |
B | PHE406 |
B | HOH611 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10008 |
Chain | Residue | Details |
A | GLU215 | |
A | ZBZ249 | |
B | GLU215 | |
B | ZBZ249 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU215 | |
A | ZBZ249 | |
A | GLU337 | |
B | GLY117 | |
B | LYS143 | |
B | ARG175 | |
B | GLY193 | |
B | GLU215 | |
B | ZBZ249 | |
B | GLU337 | |
A | GLY117 | |
A | LYS143 | |
A | ARG175 | |
A | GLY193 |