Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| C | TYR192-HIS198 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA41 | |
| A | PRO224 | |
| B | ALA41 | |
| B | PRO224 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE162 | |
| A | SER170 | |
| A | GLU312 | |
| A | GLU316 | |
| B | PHE162 | |
| B | SER170 | |
| B | GLU312 | |
| B | GLU316 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL102 | |
| B | VAL102 | |
| Chain | Residue | Details |
| A | GLN277 | |
| A | VAL326 | |
| B | GLN277 | |
| B | VAL326 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | SER35 | |
| A | LYS218 | |
| A | ASP32 | |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP215 | |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | PHE75 | |
| A | SER35 | |
| A | ASP32 | |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP215 | |
| B | PHE75 | |
| B | SER35 | |
| B | ASP32 | |
| site_id | CSA13 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP32 | |
| site_id | CSA14 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP32 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP215 | |
| B | SER35 | |
| B | LYS218 | |
| B | ASP32 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | THR216 | |
| A | ASP32 | |
| A | SER33 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP215 | |
| B | THR216 | |
| B | ASP32 | |
| B | SER33 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | SER35 | |
| A | ASP32 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP215 | |
| B | SER35 | |
| B | ASP32 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
| A | PHE75 | |
| A | SER35 | |
| A | ASP32 | |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| B | ASP215 | |
| B | PHE75 | |
| B | SER35 | |
| B | ASP32 | |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1am5 |
| Chain | Residue | Details |
| A | ASP215 | |
