5TJR
X-ray Crystal structure of a methylmalonate semialdehyde dehydrogenase from Pseudomonas sp. AAC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue ADP A 501 |
| Chain | Residue |
| A | THR146 |
| A | TYR231 |
| A | PRO147 |
| A | PHE148 |
| A | LYS172 |
| A | GLU175 |
| A | ASP204 |
| A | LYS205 |
| A | SER225 |
| A | ILE228 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue ADP B 501 |
| Chain | Residue |
| B | THR146 |
| B | PHE148 |
| B | ASN149 |
| B | LYS172 |
| B | PRO173 |
| B | GLU175 |
| B | VAL208 |
| B | GLY224 |
| B | SER225 |
| B | ILE228 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue ADP D 501 |
| Chain | Residue |
| D | ILE145 |
| D | THR146 |
| D | PRO147 |
| D | PHE148 |
| D | LYS172 |
| D | PRO173 |
| D | GLU175 |
| D | ARG176 |
| D | LYS205 |
| D | SER225 |
| D | ILE228 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue ADP E 501 |
| Chain | Residue |
| E | THR146 |
| E | PRO147 |
| E | PHE148 |
| E | ASN149 |
| E | LYS172 |
| E | SER174 |
| E | GLU175 |
| E | LYS205 |
| E | VAL208 |
| E | SER225 |
| E | ILE228 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue ADP F 501 |
| Chain | Residue |
| F | THR146 |
| F | PHE148 |
| F | LYS172 |
| F | PRO173 |
| F | SER174 |
| F | GLU175 |
| F | ARG176 |
| F | LYS205 |
| F | VAL208 |
| F | PHE222 |
| F | SER225 |
| F | ILE228 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgSCGERCMAIS |
| Chain | Residue | Details |
| A | TYR273-SER284 |
