8SUT
Crystal structure of YisK from Bacillus subtilis in complex with reaction product 4-Hydroxy-2-oxoglutaric acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050163 | molecular_function | oxaloacetate tautomerase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050163 | molecular_function | oxaloacetate tautomerase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38047707","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SKY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38047707","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SKY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SUT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SUU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
