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 | 19 |
| Details | binding site for residue GHJ A 401 |
| Chain | Residue |
| A | GLY11 |
| A | GLN73 |
| A | PHE108 |
| A | ILE110 |
| A | ILE126 |
| A | TYR198 |
| A | ASP228 |
| A | GLY230 |
| A | THR231 |
| A | THR232 |
| A | HOH545 |
| A | GLN12 |
| A | GLY13 |
| A | LEU30 |
| A | ASP32 |
| A | GLY34 |
| A | PRO70 |
| A | TYR71 |
| A | THR72 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | GLY372 |
| A | HOH542 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | SER10 |
| A | GLY11 |
| A | GLN12 |
| A | VAL309 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | ASP4 |
| A | GLN153 |
| A | SER173 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue URE A 405 |
| Chain | Residue |
| A | THR185 |
| A | GLY186 |
| C | LYS65 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue URE A 406 |
| Chain | Residue |
| A | GLU219 |
| A | TYR222 |
| A | LYS239 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue URE A 407 |
| Chain | Residue |
| A | HIS89 |
| A | HOH526 |
| C | LYS107 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue GHJ B 401 |
| Chain | Residue |
| B | GLY11 |
| B | GLN12 |
| B | GLY13 |
| B | LEU30 |
| B | ASP32 |
| B | GLY34 |
| B | SER35 |
| B | PRO70 |
| B | TYR71 |
| B | THR72 |
| B | GLN73 |
| B | PHE108 |
| B | ILE110 |
| B | ILE126 |
| B | TYR198 |
| B | ASP228 |
| B | GLY230 |
| B | THR231 |
| B | THR232 |
| B | HOH521 |
| B | HOH526 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | TYR286 |
| B | VAL375 |
| B | THR376 |
| C | THR292 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 403 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | ARG349 |
| B | ARG351 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue URE B 405 |
| Chain | Residue |
| B | THR82 |
| B | ARG96 |
| B | ASN98 |
| B | GLU134 |
| site_id | AD4 |
| Number of Residues | 18 |
| Details | binding site for residue GHJ C 401 |
| Chain | Residue |
| C | GLY11 |
| C | GLN12 |
| C | LEU30 |
| C | ASP32 |
| C | GLY34 |
| C | SER35 |
| C | PRO70 |
| C | TYR71 |
| C | THR72 |
| C | GLN73 |
| C | TYR198 |
| C | ASP228 |
| C | GLY230 |
| C | THR231 |
| C | THR232 |
| C | ARG235 |
| C | HOH536 |
| C | HOH540 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| C | LYS9 |
| C | SER10 |
| C | GLY11 |
| C | GLN12 |
| C | GLY13 |
| C | TYR14 |
| C | VAL170 |
| C | THR232 |
| C | GLU339 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | MET215 |
| C | VAL204 |
| C | ARG205 |
| C | ASP212 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | HIS45 |
| C | PHE47 |
| C | SER105 |
| C | ASP106 |
| C | LYS107 |
| C | PHE108 |
| C | PHE109 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 405 |
| Chain | Residue |
| C | ARG349 |
| C | ARG351 |
| C | HOH524 |
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"}]} |
