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 | 4 |
Details | binding site for residue NA A 101 |
Chain | Residue |
A | ASP60 |
A | HOH201 |
A | HOH218 |
A | HOH231 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL A 102 |
Chain | Residue |
A | THR74 |
A | ASN88 |
B | ARG41 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 103 |
Chain | Residue |
A | HOH227 |
B | GLN61 |
B | GLN92 |
B | HOH1118 |
B | HOH1132 |
A | LYS45 |
A | MET46 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL A 104 |
Chain | Residue |
A | LYS14 |
A | ILE15 |
A | GLY16 |
A | GLY17 |
A | ILE63 |
A | LYS70 |
site_id | AC5 |
Number of Residues | 31 |
Details | binding site for residue G52 B 201 |
Chain | Residue |
A | ARG8 |
A | ASP25 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | GLY48 |
A | GLY49 |
A | ILE50 |
A | PRO81 |
A | VAL82 |
A | ILE84 |
A | HOH206 |
A | HOH245 |
B | LEU23 |
B | ASP25 |
B | GLY27 |
B | ALA28 |
B | ASP29 |
B | ASP30 |
B | VAL32 |
B | GLY48 |
B | GLY49 |
B | ILE50 |
B | PRO81 |
B | VAL82 |
B | ILE84 |
B | HOH1102 |
B | HOH1124 |
B | HOH1142 |
B | HOH1147 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue NA B 202 |
Chain | Residue |
B | ASP60 |
B | GOL208 |
B | HOH1123 |
B | HOH1155 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL B 203 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CL B 204 |
Chain | Residue |
B | GLY73 |
B | THR74 |
B | ASN88 |
B | HOH1131 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue CL B 205 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue CL B 206 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 207 |
Chain | Residue |
A | TRP6 |
B | ASP29 |
B | ARG87 |
B | ASN88 |
B | HOH1122 |
B | HOH1133 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue GOL B 208 |
Chain | Residue |
B | ARG41 |
B | LYS43 |
B | GLN58 |
B | TYR59 |
B | ASP60 |
B | NA202 |
B | HOH1101 |
B | HOH1123 |
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 | ASP25 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | PHE99 | |
B | PHE99 | |
Catalytic Information from CSA
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 |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 175 |
Chain | Residue | Details |
B | ASP25 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | THR26 | electrostatic stabiliser, transition state stabiliser |
B | GLY27 | electrostatic stabiliser, hydrogen bond donor |