Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ROC A 100 |
Chain | Residue |
A | ARG8 |
A | VAL48 |
A | GLY49 |
A | ILE50 |
A | ILE50 |
A | PRO81 |
A | PRO81 |
A | VAL82 |
A | VAL82 |
A | ILE84 |
A | ILE84 |
A | ASP25 |
A | HOH101 |
A | HOH101 |
A | HOH102 |
A | ASP25 |
A | GLY27 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | VAL48 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL |
Chain | Residue | Details |
A | ALA22-LEU33 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP25 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | PHE99 | |
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 | 1 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 175 |
Chain | Residue | Details |
A | ASP25 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | THR26 | electrostatic stabiliser, transition state stabiliser |
A | GLY27 | electrostatic stabiliser, hydrogen bond donor |