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 | 27 |
Details | BINDING SITE FOR CHAIN C OF PR/RT SUBSTRATE PEPTIDE |
Chain | Residue |
A | ARG8 |
B | ARG8 |
B | ASN25 |
B | GLY27 |
B | ALA28 |
B | ASP29 |
B | ASP30 |
B | LYS45 |
B | LEU46 |
B | THR82 |
B | VAL84 |
A | ASN25 |
B | HOH149 |
B | HOH177 |
B | HOH190 |
C | HOH33 |
C | HOH123 |
C | HOH127 |
C | HOH131 |
C | HOH211 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | ARG41 |
A | HOH207 |
A | HOH236 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
C | PHE305 | |
B | ASN25 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | PHE99 | |
B | PHE99 | |