Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0016020 | cellular_component | membrane |
B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0016020 | cellular_component | membrane |
C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue GHJ A 401 |
Chain | Residue |
A | GLY11 |
A | GLN73 |
A | PHE108 |
A | ILE110 |
A | ILE126 |
A | TYR198 |
A | ASP228 |
A | GLY230 |
A | THR231 |
A | THR232 |
A | HOH545 |
A | GLN12 |
A | GLY13 |
A | LEU30 |
A | ASP32 |
A | GLY34 |
A | PRO70 |
A | TYR71 |
A | THR72 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | GLY372 |
A | HOH542 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | SER10 |
A | GLY11 |
A | GLN12 |
A | VAL309 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ASP4 |
A | GLN153 |
A | SER173 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue URE A 405 |
Chain | Residue |
A | THR185 |
A | GLY186 |
C | LYS65 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue URE A 406 |
Chain | Residue |
A | GLU219 |
A | TYR222 |
A | LYS239 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue URE A 407 |
Chain | Residue |
A | HIS89 |
A | HOH526 |
C | LYS107 |
site_id | AC8 |
Number of Residues | 21 |
Details | binding site for residue GHJ B 401 |
Chain | Residue |
B | GLY11 |
B | GLN12 |
B | GLY13 |
B | LEU30 |
B | ASP32 |
B | GLY34 |
B | SER35 |
B | PRO70 |
B | TYR71 |
B | THR72 |
B | GLN73 |
B | PHE108 |
B | ILE110 |
B | ILE126 |
B | TYR198 |
B | ASP228 |
B | GLY230 |
B | THR231 |
B | THR232 |
B | HOH521 |
B | HOH526 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | TYR286 |
B | VAL375 |
B | THR376 |
C | THR292 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue GOL B 403 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | ARG349 |
B | ARG351 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue URE B 405 |
Chain | Residue |
B | THR82 |
B | ARG96 |
B | ASN98 |
B | GLU134 |
site_id | AD4 |
Number of Residues | 18 |
Details | binding site for residue GHJ C 401 |
Chain | Residue |
C | GLY11 |
C | GLN12 |
C | LEU30 |
C | ASP32 |
C | GLY34 |
C | SER35 |
C | PRO70 |
C | TYR71 |
C | THR72 |
C | GLN73 |
C | TYR198 |
C | ASP228 |
C | GLY230 |
C | THR231 |
C | THR232 |
C | ARG235 |
C | HOH536 |
C | HOH540 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue GOL C 402 |
Chain | Residue |
C | LYS9 |
C | SER10 |
C | GLY11 |
C | GLN12 |
C | GLY13 |
C | TYR14 |
C | VAL170 |
C | THR232 |
C | GLU339 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue GOL C 403 |
Chain | Residue |
C | MET215 |
C | VAL204 |
C | ARG205 |
C | ASP212 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue GOL C 404 |
Chain | Residue |
C | HIS45 |
C | PHE47 |
C | SER105 |
C | ASP106 |
C | LYS107 |
C | PHE108 |
C | PHE109 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 405 |
Chain | Residue |
C | ARG349 |
C | ARG351 |
C | HOH524 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV |
Chain | Residue | Details |
A | ILE29-VAL40 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP32 | |
A | ASP228 | |
B | ASP32 | |
B | ASP228 | |
C | ASP32 | |
C | ASP228 | |
Chain | Residue | Details |
A | LYS65 | |
B | LYS218 | |
B | LYS224 | |
B | LYS238 | |
B | LYS239 | |
B | LYS246 | |
C | LYS65 | |
C | LYS214 | |
C | LYS218 | |
C | LYS224 | |
C | LYS238 | |
A | LYS214 | |
C | LYS239 | |
C | LYS246 | |
A | LYS218 | |
A | LYS224 | |
A | LYS238 | |
A | LYS239 | |
A | LYS246 | |
B | LYS65 | |
B | LYS214 | |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN92 | |
C | ASN111 | |
C | ASN162 | |
C | ASN293 | |
A | ASN111 | |
A | ASN162 | |
A | ASN293 | |
B | ASN92 | |
B | ASN111 | |
B | ASN162 | |
B | ASN293 | |
C | ASN92 | |