3HSK
Crystal Structure of Aspartate Semialdehyde Dehydrogenase with NADP from Candida albicans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009088 | biological_process | L-threonine biosynthetic process |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009088 | biological_process | L-threonine biosynthetic process |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAP A 366 |
| Chain | Residue |
| A | GLY10 |
| A | ASP86 |
| A | VAL89 |
| A | GLY194 |
| A | THR12 |
| A | GLY13 |
| A | SER14 |
| A | ALA36 |
| A | SER37 |
| A | SER40 |
| A | GLY84 |
| A | LEU85 |
Functional Information from PROSITE/UniProt
| site_id | PS01103 |
| Number of Residues | 15 |
| Details | ASD Aspartate-semialdehyde dehydrogenase signature. VSaqCnRVpvidGHT |
| Chain | Residue | Details |
| A | VAL243-THR257 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"PIRSR","id":"PIRSR000148-1","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PIRSR","id":"PIRSR000148-1","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24025428","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HSK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A179UL48","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A080WMA9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
