5X5U
Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (KGSADH) complexed with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic 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 | 0019568 | biological_process | arabinose catabolic process |
| A | 0019570 | biological_process | L-arabinose catabolic process to 2-oxoglutarate |
| A | 0047533 | molecular_function | 2,5-dioxovalerate dehydrogenase (NADP+) activity |
| A | 0051262 | biological_process | protein tetramerization |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009450 | biological_process | gamma-aminobutyric acid catabolic 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 | 0019568 | biological_process | arabinose catabolic process |
| B | 0019570 | biological_process | L-arabinose catabolic process to 2-oxoglutarate |
| B | 0047533 | molecular_function | 2,5-dioxovalerate dehydrogenase (NADP+) activity |
| B | 0051262 | biological_process | protein tetramerization |
| B | 0070401 | molecular_function | NADP+ binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | PRO153 |
| A | VAL235 |
| A | GLU253 |
| A | LEU254 |
| A | CYS287 |
| A | ARG333 |
| A | ARG334 |
| A | GLU384 |
| A | PHE386 |
| A | HOH642 |
| A | HOH697 |
| A | TRP154 |
| A | HOH759 |
| A | HOH767 |
| A | ASN155 |
| A | GLN160 |
| A | PRO211 |
| A | ALA212 |
| A | SER215 |
| A | GLY231 |
| A | SER232 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ASP19 |
| A | ALA20 |
| A | ALA21 |
| A | GLY23 |
| A | GLU83 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | PRO153 |
| B | TRP154 |
| B | GLN160 |
| B | PRO211 |
| B | ALA212 |
| B | SER215 |
| B | PHE229 |
| B | GLY231 |
| B | SER232 |
| B | VAL235 |
| B | GLU253 |
| B | LEU254 |
| B | CYS287 |
| B | ARG333 |
| B | ARG334 |
| B | GLU384 |
| B | PHE386 |
| B | HOH639 |
| B | HOH647 |
| B | HOH714 |
| B | HOH724 |
| B | HOH733 |
| B | HOH765 |
| B | HOH774 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU253 | |
| B | GLU253 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS287 | |
| B | CYS287 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY231 | |
| A | LEU254 | |
| A | GLU384 | |
| B | TRP154 | |
| B | LYS178 | |
| B | GLY231 | |
| B | LEU254 | |
| B | GLU384 | |
| A | TRP154 | |
| A | LYS178 |
