1LYA
CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN CATHEPSIN D: IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG DESIGN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNLWV |
Chain | Residue | Details |
A | VAL30-VAL41 | |
B | ALA228-GLY239 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:8393577 |
Chain | Residue | Details |
B | ASP231 | |
D | ASP231 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:8393577 |
Chain | Residue | Details |
B | ASN199 | |
D | ASN199 |