Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 602 |
Chain | Residue |
A | HIS131 |
A | ASP191 |
A | HIS197 |
A | ASP214 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR CHAIN B OF PEPSTATIN A |
Chain | Residue |
A | TYR84 |
A | GLY85 |
A | ASP86 |
A | ASP218 |
A | GLY220 |
A | THR221 |
A | THR222 |
A | TYR303 |
A | HOH2005 |
A | HOH2212 |
B | HOH2106 |
B | HOH2147 |
B | HOH2218 |
B | HOH2319 |
A | VAL12 |
A | ASP32 |
A | GLY34 |
A | SER35 |
A | GLU83 |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVIDTGSSDLWV |
Chain | Residue | Details |
A | VAL29-VAL40 | |
A | VAL215-LEU226 | |
site_id | PS00307 |
Number of Residues | 7 |
Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. LTVVIDT |
Chain | Residue | Details |
A | LEU27-THR33 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 312 |
Details | Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 15 |
Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17510964","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H6T","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"2H6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H6T","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP32 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP218 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | THR221 | |
A | SER35 | |
A | ASP218 | |
A | ASP32 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | ASP218 | |
A | ASP32 | |
A | THR33 | |
A | SER219 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | SER35 | |
A | ASP218 | |
A | ASP32 | |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | SER35 | |
A | TYR84 | |
A | ASP218 | |
A | ASP32 | |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1am5 |
Chain | Residue | Details |
A | THR221 | |
A | ASP218 | |
A | ASP32 | |
A | THR33 | |