1MC4
Crystal Structure of Aspartate-Semialdehyde dehydrogenase from Vibrio Cholerae El Tor
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 PROSITE/UniProt
| site_id | PS01103 |
| Number of Residues | 15 |
| Details | ASD Aspartate-semialdehyde dehydrogenase signature. IDgtCvRIgamrCHS |
| Chain | Residue | Details |
| A | ILE261-SER275 |
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":"12493825","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":"12493825","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12493825","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02121","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12493825","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-cysteinyl cysteine; in inhibited form"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1brm |
| Chain | Residue | Details |
| A | HIS274 | |
| A | CYS134 | |
| A | GLN161 |
