Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE KNI B 900 |
Chain | Residue |
A | ARG8 |
B | ASP125 |
B | GLY127 |
B | ALA128 |
B | ASP129 |
B | ASP130 |
B | VAL132 |
B | GLY148 |
B | GLY149 |
B | ILE150 |
B | DOD301 |
A | ASP25 |
A | GLY27 |
A | ALA28 |
A | GLY48 |
A | GLY49 |
A | ILE50 |
A | PRO81 |
A | ILE84 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI |
Chain | Residue | Details |
A | ALA22-ILE33 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP25 | |
B | ASP125 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | PHE99 | |
B | PHE199 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
A | THR26 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
B | THR126 | |
B | ASP125 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
B | ASP125 | |