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 | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:9891971 |
| Chain | Residue | Details |
| A | HIS150 | |
| B | HIS150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:9891971 |
| Chain | Residue | Details |
| A | CYS191 | |
| B | CYS191 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by autolysis |
| Chain | Residue | Details |
| A | ASN325 | |
| B | ASN325 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN93 | |
| A | ASN169 | |
| A | ASN265 | |
| A | ASN274 | |
| B | ASN93 | |
| B | ASN169 | |
| B | ASN265 | |
| B | ASN274 |
