4NOL
Crystal structure of proenzyme asparaginyl endopeptidase (AEP)/Legumain mutant D233A at pH 7.5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0051603 | biological_process | proteolysis involved in protein catabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9891971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9891971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by autolysis"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
