1PQP
Crystal Structure of the C136S Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae Bound with Aspartate Semialdehyde and Phosphate
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 PO4 A 2902 |
| Chain | Residue |
| A | ARG103 |
| A | ASN135 |
| A | SER136 |
| A | LYS246 |
| A | HSE372 |
| A | HOH2905 |
| A | HOH2987 |
| A | HOH3060 |
| A | HOH3109 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HSE A 372 |
| Chain | Residue |
| A | SER136 |
| A | GLN163 |
| A | GLY167 |
| A | ARG270 |
| A | HIS277 |
| A | GLN353 |
| A | PO42902 |
| A | HOH2938 |
| A | HOH2986 |
| A | HOH2987 |
| A | HOH3060 |
Functional Information from PROSITE/UniProt
| site_id | PS01103 |
| Number of Residues | 15 |
| Details | ASD Aspartate-semialdehyde dehydrogenase signature. VDglCvRIgalrCHS |
| Chain | Residue | Details |
| A | VAL264-SER278 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161 |
| Chain | Residue | Details |
| A | SER136 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:14559965 |
| Chain | Residue | Details |
| A | HIS277 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15272161 |
| Chain | Residue | Details |
| A | ARG10 | |
| A | THR37 | |
| A | GLN74 | |
| A | SER166 | |
| A | GLN353 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14559965 |
| Chain | Residue | Details |
| A | ARG103 | |
| A | LYS246 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15272161 |
| Chain | Residue | Details |
| A | GLN163 | |
| A | GLU243 | |
| A | ARG270 |
