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 | 23 |
Details | BINDING SITE FOR CHAIN X OF NVP-AMK640 INHIBITOR |
Chain | Residue |
A | GLY11 |
A | ASP228 |
A | GLY230 |
A | THR231 |
A | THR232 |
A | ARG235 |
A | ARG307 |
A | LYS321 |
A | HOH1028 |
A | HOH1090 |
X | HOH1012 |
A | ASP32 |
X | HOH1091 |
X | HOH1165 |
X | HOH1172 |
X | HOH1192 |
A | GLY34 |
A | TYR71 |
A | THR72 |
A | GLN73 |
A | ILE110 |
A | ARG128 |
A | TYR198 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR CHAIN Y OF NVP-AMK640 INHIBITOR |
Chain | Residue |
B | GLY11 |
B | GLN12 |
B | GLY13 |
B | ASP32 |
B | GLY34 |
B | TYR71 |
B | THR72 |
B | GLN73 |
B | ILE110 |
B | TYR198 |
B | ASP228 |
B | GLY230 |
B | THR231 |
B | THR232 |
B | ARG235 |
B | ARG307 |
B | ASP311 |
B | ALA313 |
B | HOH2026 |
B | HOH2062 |
Y | HOH2035 |
Y | HOH2139 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR CHAIN Z OF NVP-AMK640 INHIBITOR |
Chain | Residue |
C | GLY11 |
C | GLN12 |
C | LEU30 |
C | ASP32 |
C | PRO70 |
C | TYR71 |
C | THR72 |
C | GLN73 |
C | ILE110 |
C | TYR198 |
C | ASP228 |
C | GLY230 |
C | THR231 |
C | THR232 |
C | ARG235 |
C | ARG307 |
C | HOH3003 |
Z | HOH3076 |
Z | HOH3094 |
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 | |