8RJ0
Crystal structure of mutant aspartase from Bacillus sp. YM55-1 in the closed loop conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0008797 | molecular_function | aspartate ammonia-lyase activity |
| A | 0016829 | molecular_function | lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0008797 | molecular_function | aspartate ammonia-lyase activity |
| B | 0016829 | molecular_function | lyase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Region: {"description":"SS loop","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21661762","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3R6V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
