Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
Chain | Residue |
A | ASP57 |
A | GLU324 |
A | HOH672 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE A70 A 500 |
Chain | Residue |
A | GLY34 |
A | TYR84 |
A | GLY85 |
A | ASP86 |
A | ILE119 |
A | ILE123 |
A | ASN131 |
A | GLU193 |
A | ASP218 |
A | GLY220 |
A | THR221 |
A | THR222 |
A | ASN301 |
A | ILE305 |
A | HOH632 |
A | HOH902 |
A | VAL12 |
A | THR13 |
A | ILE30 |
A | ASP32 |
site_id | ACT |
Number of Residues | 2 |
Details | ASPARTIC PROTEINASES ARE CHARACTERIZED BY TWO ASP RESIDUES, ONE FROM EACH DOMAIN, CORRESPONDING TO PEPSIN ASP 32, ASP 218. |
Chain | Residue |
A | ASP32 |
A | ASP218 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIVDTGSSDLWV |
Chain | Residue | Details |
A | VAL29-VAL40 | |
A | VAL215-LEU226 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP32 | |
A | ASP218 | |
Chain | Residue | Details |
A | ASP32 | |
A | GLY85 | |
A | ASP191 | |
A | ASP214 | |
A | ASP218 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN257 | |
A | ASN265 | |