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 | 10 |
| Details | BINDING SITE FOR RESIDUE EV3 A 393 |
| Chain | Residue |
| A | ASP32 |
| A | HOH613 |
| A | GLY34 |
| A | VAL69 |
| A | TYR71 |
| A | TRP76 |
| A | ILE226 |
| A | ASP228 |
| A | GOL398 |
| A | GOL399 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 394 |
| Chain | Residue |
| A | ASP4 |
| A | ASN5 |
| A | ARG7 |
| A | HOH529 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 395 |
| Chain | Residue |
| A | THR231 |
| A | THR232 |
| A | ASN233 |
| A | ARG235 |
| A | SER325 |
| A | GOL399 |
| A | HOH466 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 396 |
| Chain | Residue |
| A | ASN209 |
| A | GLY210 |
| A | VAL282 |
| A | HOH583 |
| C | ASN209 |
| C | ARG366 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 397 |
| Chain | Residue |
| A | LYS218 |
| A | GLU219 |
| A | TYR222 |
| A | TYR384 |
| A | HOH622 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 398 |
| Chain | Residue |
| A | LEU30 |
| A | PHE108 |
| A | ILE118 |
| A | GLY230 |
| A | EV3393 |
| A | GOL399 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 399 |
| Chain | Residue |
| A | THR231 |
| A | ARG235 |
| A | VAL332 |
| A | EV3393 |
| A | GOL395 |
| A | GOL398 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 400 |
| Chain | Residue |
| A | SER187 |
| A | LEU188 |
| A | HOH634 |
| C | ARG64 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EV3 B 393 |
| Chain | Residue |
| B | ASP32 |
| B | GLY34 |
| B | TYR71 |
| B | TRP76 |
| B | ILE226 |
| B | ASP228 |
| B | GOL401 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 394 |
| Chain | Residue |
| A | ASN98 |
| A | SER132 |
| A | GLU134 |
| B | PHE-1 |
| B | SER-2 |
| B | VAL0 |
| B | GLU1 |
| B | HOH536 |
| B | HOH613 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 395 |
| Chain | Residue |
| B | SER86 |
| B | ILE87 |
| B | PRO88 |
| B | ASN92 |
| B | VAL93 |
| B | THR94 |
| B | HOH446 |
| B | HOH640 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 396 |
| Chain | Residue |
| B | VAL3 |
| B | ASP4 |
| B | ASN5 |
| B | HIS89 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 397 |
| Chain | Residue |
| B | LYS9 |
| B | GLY11 |
| B | GLY13 |
| B | VAL170 |
| B | THR232 |
| B | GLU339 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 398 |
| Chain | Residue |
| B | THR19 |
| B | VAL20 |
| B | GLY21 |
| B | SER22 |
| B | PRO24 |
| B | LEU84 |
| B | SER86 |
| B | THR94 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 399 |
| Chain | Residue |
| B | GLU77 |
| B | GLU104 |
| B | SER105 |
| B | HOH544 |
| C | ASP131 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 400 |
| Chain | Residue |
| B | LYS214 |
| B | MET215 |
| B | TYR220 |
| B | HOH552 |
| B | HOH600 |
| B | VAL204 |
| B | ARG205 |
| B | VAL206 |
| B | ASP212 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 401 |
| Chain | Residue |
| B | LEU30 |
| B | PHE108 |
| B | EV3393 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EV3 C 393 |
| Chain | Residue |
| C | ASP32 |
| C | GLY34 |
| C | TYR71 |
| C | TRP76 |
| C | PHE108 |
| C | ILE226 |
| C | ASP228 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 394 |
| Chain | Residue |
| C | THR231 |
| C | THR232 |
| C | ASN233 |
| C | HOH485 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 395 |
| Chain | Residue |
| C | SER187 |
| C | LEU188 |
| C | TRP189 |
| C | HOH430 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
