5V2I
Crystal structure of a mutant glycosylasparaginase (G172D) that causes the genetic disease Aspartylglucosaminuria
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003948 | molecular_function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0042597 | cellular_component | periplasmic space |
| B | 0003948 | molecular_function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0042597 | cellular_component | periplasmic space |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10490104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17157318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20800597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9685368","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
