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 | 14 |
Details | binding site for residue E4J A 401 |
Chain | Residue |
A | SER10 |
A | PHE108 |
A | ASP228 |
A | GLY230 |
A | THR231 |
A | ARG235 |
A | GLY11 |
A | GLN12 |
A | GLY13 |
A | ASP32 |
A | GLY34 |
A | TYR71 |
A | THR72 |
A | GLN73 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | THR72 |
A | ARG235 |
A | GLN326 |
A | SER328 |
A | THR329 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue E4J B 401 |
Chain | Residue |
B | SER10 |
B | GLY11 |
B | GLY13 |
B | LEU30 |
B | ASP32 |
B | GLY34 |
B | PRO70 |
B | TYR71 |
B | THR72 |
B | GLN73 |
B | PHE108 |
B | ASP228 |
B | GLY230 |
B | THR232 |
B | HOH509 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
B | THR72 |
B | ARG235 |
B | SER327 |
B | SER328 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue E4J C 401 |
Chain | Residue |
C | SER10 |
C | GLY11 |
C | GLY13 |
C | ASP32 |
C | GLY34 |
C | TYR71 |
C | THR72 |
C | GLN73 |
C | PHE108 |
C | ASP228 |
C | GLY230 |
C | THR231 |
C | THR232 |
C | ARG235 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 402 |
Chain | Residue |
C | ARG235 |
C | SER327 |
C | SER328 |
C | THR329 |
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 | |