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 |
C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 29 |
Details | BINDING SITE FOR CHAIN E OF INHIBITOR BI-LA-398 |
Chain | Residue |
A | ASP25 |
A | ILE50 |
A | PRO81 |
A | ILE82 |
A | ILE84 |
B | ARG8 |
B | ASP25 |
B | GLY27 |
B | ASP29 |
B | GLY48 |
B | GLY49 |
A | GLY27 |
B | ILE50 |
D | TYR14 |
E | HOH501 |
G | PHE1 |
G | VAL2 |
G | PHE3 |
G | LEU4 |
G | GLU5 |
G | ILE6 |
G | NH27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | ILE32 |
A | VAL47 |
A | GLY48 |
A | GLY49 |
site_id | AC2 |
Number of Residues | 31 |
Details | BINDING SITE FOR CHAIN F OF INHIBITOR BI-LA-398 |
Chain | Residue |
B | ASN40 |
B | ASN41 |
B | GLU65 |
C | LEU23 |
C | ASP25 |
C | GLY27 |
C | ALA28 |
C | ASP29 |
C | GLY48 |
C | GLY49 |
C | ILE50 |
C | ILE82 |
C | ILE84 |
D | ASP25 |
D | GLY27 |
D | ALA28 |
D | ASP29 |
D | ASP30 |
D | VAL47 |
D | GLY48 |
D | GLY49 |
D | PRO81 |
D | ILE82 |
F | HOH701 |
H | PHE1 |
H | VAL2 |
H | PHE3 |
H | LEU4 |
H | GLU5 |
H | ILE6 |
H | NH27 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR CHAIN G OF INHIBITOR BI-LA-398 |
Chain | Residue |
A | ASP25 |
A | GLY27 |
A | ALA28 |
A | ASP29 |
A | ASP30 |
A | GLY48 |
A | GLY49 |
A | ILE50 |
A | PRO81 |
A | ILE84 |
B | ARG8 |
B | ASP25 |
B | GLY27 |
B | ALA28 |
B | ASP29 |
B | ASP30 |
B | VAL47 |
B | GLY48 |
B | ILE50 |
B | HOH505 |
E | PHE1 |
E | VAL2 |
E | PHE3 |
E | LEU4 |
E | GLU5 |
E | ILE6 |
E | NH27 |
E | HOH501 |
site_id | AC4 |
Number of Residues | 32 |
Details | BINDING SITE FOR CHAIN H OF INHIBITOR BI-LA-398 |
Chain | Residue |
C | GLY49 |
C | ILE50 |
C | ILE82 |
D | ASP25 |
D | GLY27 |
D | ALA28 |
D | ASP29 |
D | VAL47 |
D | GLY48 |
D | GLY49 |
D | ILE50 |
D | PRO81 |
D | ILE82 |
F | PHE1 |
F | VAL2 |
F | PHE3 |
F | LEU4 |
F | GLU5 |
F | ILE6 |
F | NH27 |
F | HOH701 |
B | TYR14 |
B | ASN40 |
B | ASN41 |
B | TYR42 |
C | ASP25 |
C | GLY27 |
C | ALA28 |
C | ASP29 |
C | ASP30 |
C | VAL47 |
C | GLY48 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLLDTGADDSIV |
Chain | Residue | Details |
A | VAL22-VAL33 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
A | ILE50 | |
B | ILE50 | |
C | ILE50 | |
D | ILE50 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by host => ECO:0000250 |
Chain | Residue | Details |
A | ILE50 | |
B | ILE50 | |
C | ILE50 | |
D | ILE50 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
A | THR26 | |
B | ASP25 | |
B | THR26 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
D | ASP25 | |
D | THR26 | |
C | ASP25 | |
C | THR26 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
A | ASP25 | |
B | ASP25 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a30 |
Chain | Residue | Details |
C | ASP25 | |
D | ASP25 | |