3PWS
Crystal Structure of Aspartate beta-Semialdehide Dehydrogenase from Streptococcus pneumoniae with 2',5'-Adenosine diphosphate and D-2-aminoadipate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | L-lysine biosynthetic process |
| A | 0009088 | biological_process | L-threonine biosynthetic process |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 1901705 | biological_process | L-isoleucine biosynthetic process |
| B | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009085 | biological_process | L-lysine biosynthetic process |
| B | 0009088 | biological_process | L-threonine biosynthetic process |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 1901705 | biological_process | L-isoleucine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 11C A 367 |
| Chain | Residue |
| A | ARG99 |
| A | ASN127 |
| A | CYS128 |
| A | GLN155 |
| A | GLY159 |
| A | ILE209 |
| A | GLU220 |
| A | LYS223 |
| A | ARG245 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 368 |
| Chain | Residue |
| A | ALA274 |
| A | PHE276 |
| A | ALA279 |
| B | GLU343 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE A2P A 369 |
| Chain | Residue |
| A | GLY9 |
| A | THR11 |
| A | GLY12 |
| A | ALA13 |
| A | ALA36 |
| A | SER37 |
| A | ARG39 |
| A | SER40 |
| A | THR57 |
| A | ALA72 |
| A | THR76 |
| A | GLY161 |
| A | MET162 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 11C B 367 |
| Chain | Residue |
| B | ARG99 |
| B | ASN127 |
| B | CYS128 |
| B | GLN155 |
| B | GLY159 |
| B | ILE209 |
| B | GLU220 |
| B | LYS223 |
| B | ARG245 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE A2P B 368 |
| Chain | Residue |
| B | GLY9 |
| B | THR11 |
| B | GLY12 |
| B | ALA13 |
| B | ALA36 |
| B | SER37 |
| B | ARG39 |
| B | SER40 |
| B | THR57 |
| B | ALA72 |
| B | THR76 |
| B | GLY161 |
| B | MET162 |
