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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 501 |
Chain | Residue |
A | SER105 |
A | HOH565 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD A 502 |
Chain | Residue |
A | HIS45 |
A | PHE47 |
A | LYS107 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS A 503 |
Chain | Residue |
A | SER139 |
A | GLN143 |
A | HOH741 |
A | ARG96 |
A | ALA97 |
A | ASN98 |
A | GLU134 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 8IP A 504 |
Chain | Residue |
A | GLY11 |
A | ASP32 |
A | GLY34 |
A | GLN73 |
A | LYS107 |
A | PHE108 |
A | ASP228 |
A | GLY230 |
A | THR231 |
A | HOH760 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 505 |
Chain | Residue |
A | LYS9 |
A | SER10 |
A | GLY11 |
A | GLN12 |
A | GLY13 |
A | TYR14 |
A | ARG307 |
A | ALA335 |
A | GLU339 |
A | HOH658 |
A | HOH730 |
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 | |
Chain | Residue | Details |
A | LYS65 | |
A | LYS214 | |
A | LYS218 | |
A | LYS224 | |
A | LYS238 | |
A | LYS239 | |
A | LYS246 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN92 | |
A | ASN111 | |
A | ASN162 | |
A | ASN293 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP32 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP228 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | THR231 | |
A | ASP228 | |
A | SER35 | |
A | ASP32 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP228 | |
A | SER229 | |
A | ASP32 | |
A | THR33 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP228 | |
A | SER35 | |
A | ASP32 | |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP228 | |
A | SER35 | |
A | TYR71 | |
A | ASP32 | |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | THR231 | |
A | ASP228 | |
A | ASP32 | |
A | THR33 | |