1NX6
Crystal Structure of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae as a Tetrahedral Hemithiocetal Reaction intermediate with Phosphate at 2.15 A
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 | 0009067 | biological_process | aspartate family 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 372 |
| Chain | Residue |
| A | SER100 |
| A | ARG103 |
| A | ASN135 |
| A | HTI136 |
| A | LYS246 |
| A | PO4373 |
| A | HOH421 |
| A | HOH429 |
| A | HOH471 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 373 |
| Chain | Residue |
| A | SER100 |
| A | ASP232 |
| A | LYS242 |
| A | LYS246 |
| A | PO4372 |
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 | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"14559965","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15272161","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14559965","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15272161","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14559965","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15272161","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1brm |
| Chain | Residue | Details |
| A | HIS277 | |
| A | GLN163 |
