6BAC
Crystal Structure of Aspartate-Semialdehyde Dehydrogenase from Neisseria gonorrhoeae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009097 | biological_process | isoleucine biosynthetic 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 | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | ARG9 |
| A | THR36 |
| A | SER37 |
| A | SER38 |
| A | GLN73 |
| A | HOH502 |
| A | HOH525 |
| A | HOH572 |
| A | HOH658 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | GLY168 |
| A | ALA169 |
| A | LYS170 |
| A | HOH547 |
| A | HOH597 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ASP231 |
| A | ARG268 |
| A | LYS310 |
| A | HOH532 |
| A | HOH612 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | PHE26 |
| A | ILE29 |
| A | PRO30 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | ASN39 |
| A | GLY42 |
| A | PRO113 |
| A | ASN300 |
| A | ASP301 |
| A | TRP302 |
| A | ARG362 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | GLY75 |
| A | ASP76 |
| A | HOH515 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ARG9 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | ARG365 |
| A | HOH531 |
| A | HOH574 |
| A | HOH619 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | SER210 |
| A | GLU211 |
| A | HOH584 |
Functional Information from PROSITE/UniProt
| site_id | PS01103 |
| Number of Residues | 15 |
| Details | ASD Aspartate-semialdehyde dehydrogenase signature. IDglCvRIgamrCHS |
| Chain | Residue | Details |
| A | ILE262-SER276 |
