Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0005773 | cellular_component | vacuole |
A | 0005775 | cellular_component | vacuolar lumen |
A | 0006508 | biological_process | proteolysis |
A | 0016020 | cellular_component | membrane |
A | 0020020 | cellular_component | food vacuole |
A | 0044002 | biological_process | acquisition of nutrients from host |
B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
B | 0005773 | cellular_component | vacuole |
B | 0005775 | cellular_component | vacuolar lumen |
B | 0006508 | biological_process | proteolysis |
B | 0016020 | cellular_component | membrane |
B | 0020020 | cellular_component | food vacuole |
B | 0044002 | biological_process | acquisition of nutrients from host |
C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
C | 0005773 | cellular_component | vacuole |
C | 0005775 | cellular_component | vacuolar lumen |
C | 0006508 | biological_process | proteolysis |
C | 0016020 | cellular_component | membrane |
C | 0020020 | cellular_component | food vacuole |
C | 0044002 | biological_process | acquisition of nutrients from host |
D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
D | 0005773 | cellular_component | vacuole |
D | 0005775 | cellular_component | vacuolar lumen |
D | 0006508 | biological_process | proteolysis |
D | 0016020 | cellular_component | membrane |
D | 0020020 | cellular_component | food vacuole |
D | 0044002 | biological_process | acquisition of nutrients from host |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE K95 A 329 |
Chain | Residue |
A | HIS32 |
A | ALA34 |
A | SER35 |
A | LEU128 |
A | LEU291 |
A | HOH350 |
A | HOH607 |
B | GLU278 |
B | HOH364 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE K95 C 329 |
Chain | Residue |
C | HIS32 |
C | ALA34 |
C | SER35 |
C | LEU128 |
C | ASP215 |
C | GLU292 |
C | HOH365 |
D | GLU278 |
D | ALA280 |
D | HOH666 |
D | HOH710 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE K95 C 330 |
Chain | Residue |
C | GLU278 |
C | LEU281 |
C | HOH338 |
C | HOH556 |
C | HOH592 |
D | HIS32 |
D | ALA34 |
D | SER35 |
D | MET189 |
D | ASP215 |
D | EDO332 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA D 329 |
Chain | Residue |
B | ARG261 |
D | ARG261 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 331 |
Chain | Residue |
C | SER36 |
C | GLY122 |
C | LEU123 |
C | GLY124 |
C | PRO135 |
C | TYR136 |
C | HOH398 |
C | HOH828 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 329 |
Chain | Residue |
A | PHE111 |
A | HOH383 |
B | PRO277 |
B | GLU278 |
B | ASN279 |
B | ILE279 |
B | SER279 |
B | HOH581 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO D 330 |
Chain | Residue |
C | PHE111 |
D | PRO277 |
D | GLU278 |
D | ASN279 |
D | ILE279 |
D | SER279 |
D | HOH557 |
D | HOH600 |
D | HOH762 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 330 |
Chain | Residue |
A | LYS66 |
A | LYS100 |
A | GLN230 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 332 |
Chain | Residue |
C | GLN143 |
C | LYS145 |
D | LYS19 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 333 |
Chain | Residue |
C | PRO98 |
C | LYS145 |
D | ASP22 |
D | HOH362 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 331 |
Chain | Residue |
D | LYS100 |
D | GLU226 |
D | ASN229 |
D | GLU233 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 332 |
Chain | Residue |
C | K95330 |
D | SER35 |
D | SER36 |
D | ASN37 |
D | TRP39 |
D | LEU128 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 333 |
Chain | Residue |
C | THR63 |
C | GLU65 |
C | LYS86 |
C | PRO98 |
D | ASN23 |
D | HOH817 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 331 |
Chain | Residue |
A | SER219 |
A | GLU276 |
A | ASN285 |
B | GLU276 |
B | PG5330 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 334 |
Chain | Residue |
C | ASP67 |
C | THR69 |
C | LYS100 |
C | GLY131 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG5 B 330 |
Chain | Residue |
B | MET283 |
A | GLU276 |
A | MET283 |
A | ASN285 |
A | EDO331 |
B | VAL220 |
B | GLU276 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 D 334 |
Chain | Residue |
B | ARG261 |
D | ASP193 |
D | ASP195 |
D | LYS209 |
D | ARG261 |
D | SER262 |
D | PRO263 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 333 |
Chain | Residue |
A | PRO70 |
A | VAL71 |
A | LYS72 |
A | SER236 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 A 334 |
Chain | Residue |
A | SER95 |
A | PRO98 |
A | LYS145 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 A 335 |
Chain | Residue |
A | LYS183 |
B | ASN203 |
B | PHE238 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 336 |
Chain | Residue |
A | ASN144 |
A | LYS145 |
A | ILE146 |
A | GLU147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 144 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | MET-124-LEU-88 | |
B | MET-124-LEU-88 | |
C | MET-124-LEU-88 | |
D | MET-124-LEU-88 | |
site_id | SWS_FT_FI2 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255 |
Chain | Residue | Details |
A | PHE-87-PHE-67 | |
B | PHE-87-PHE-67 | |
C | PHE-87-PHE-67 | |
D | PHE-87-PHE-67 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1568 |
Details | TOPO_DOM: Lumenal => ECO:0000305 |
Chain | Residue | Details |
A | GLU-66-LEU328 | |
B | GLU-66-LEU328 | |
C | GLU-66-LEU328 | |
D | GLU-66-LEU328 | |
Chain | Residue | Details |
A | ASP215 | |
B | ASP215 | |
C | ASP215 | |
D | ASP215 | |