Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0016020 | cellular_component | membrane |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0016020 | cellular_component | membrane |
| C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 0K9 A 501 |
| Chain | Residue |
| A | GLY11 |
| A | TYR71 |
| A | THR72 |
| A | ILE110 |
| A | ASP228 |
| A | GLY230 |
| A | THR231 |
| A | ARG235 |
| A | THR329 |
| A | HOH624 |
| A | HOH744 |
| A | GLN12 |
| A | HOH765 |
| A | HOH920 |
| A | GLY13 |
| A | LEU30 |
| A | ASP32 |
| A | GLY34 |
| A | SER35 |
| A | VAL69 |
| A | PRO70 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | LYS9 |
| A | SER10 |
| A | GLY11 |
| A | GLN12 |
| A | GLY13 |
| A | TYR14 |
| A | GLU339 |
| A | HOH687 |
| A | HOH832 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 0K9 B 501 |
| Chain | Residue |
| B | GLY11 |
| B | GLN12 |
| B | GLY13 |
| B | LEU30 |
| B | ASP32 |
| B | GLY34 |
| B | SER35 |
| B | PRO70 |
| B | TYR71 |
| B | THR72 |
| B | PHE108 |
| B | ILE110 |
| B | TYR198 |
| B | ASP228 |
| B | GLY230 |
| B | THR231 |
| B | ARG235 |
| B | THR329 |
| B | HOH639 |
| B | HOH659 |
| B | HOH798 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| B | SER10 |
| B | GLY11 |
| B | GLN12 |
| B | GLY13 |
| B | TYR14 |
| B | GLU339 |
| B | HOH690 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | THR292 |
| B | ASP378 |
| B | HOH719 |
| B | HOH766 |
| B | HOH824 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 0K9 C 501 |
| Chain | Residue |
| C | GLY11 |
| C | GLN12 |
| C | GLY13 |
| C | LEU30 |
| C | ASP32 |
| C | GLY34 |
| C | SER35 |
| C | VAL69 |
| C | PRO70 |
| C | TYR71 |
| C | THR72 |
| C | ASP228 |
| C | GLY230 |
| C | THR231 |
| C | THR329 |
| C | HOH650 |
| C | HOH797 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 502 |
| Chain | Residue |
| C | LYS9 |
| C | SER10 |
| C | GLY11 |
| C | GLN12 |
| C | GLY13 |
| C | TYR14 |
| C | VAL170 |
| C | GLU339 |
| C | HOH698 |
| C | HOH770 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV |
| Chain | Residue | Details |
| A | ILE29-VAL40 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP32 | |
| A | ASP228 | |
| B | ASP32 | |
| B | ASP228 | |
| C | ASP32 | |
| C | ASP228 | |
| Chain | Residue | Details |
| A | LYS65 | |
| B | LYS218 | |
| B | LYS224 | |
| B | LYS238 | |
| B | LYS239 | |
| B | LYS246 | |
| C | LYS65 | |
| C | LYS214 | |
| C | LYS218 | |
| C | LYS224 | |
| C | LYS238 | |
| A | LYS214 | |
| C | LYS239 | |
| C | LYS246 | |
| A | LYS218 | |
| A | LYS224 | |
| A | LYS238 | |
| A | LYS239 | |
| A | LYS246 | |
| B | LYS65 | |
| B | LYS214 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN92 | |
| C | ASN111 | |
| C | ASN162 | |
| C | ASN293 | |
| A | ASN111 | |
| A | ASN162 | |
| A | ASN293 | |
| B | ASN92 | |
| B | ASN111 | |
| B | ASN162 | |
| B | ASN293 | |
| C | ASN92 | |
