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5UX4

Crystal Structure of Rat Cathepsin D with (5S)-3-(5,6-dihydro-2H-pyran-3-yl)-1-fluoro- 7-(2-fluoropyridin-3-yl)spiro[chromeno[2,3- c]pyridine-5,4'-[1,3]oxazol]-2'-amine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004190molecular_functionaspartic-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0006508biological_processproteolysis
A0030163biological_processprotein catabolic process
A0031667biological_processresponse to nutrient levels
A0042277molecular_functionpeptide binding
A0042470cellular_componentmelanosome
A0098830cellular_componentpresynaptic endosome
A0098982cellular_componentGABA-ergic synapse
A0099532biological_processsynaptic vesicle endosomal processing
B0004175molecular_functionendopeptidase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0005576cellular_componentextracellular region
B0005764cellular_componentlysosome
B0005768cellular_componentendosome
B0006508biological_processproteolysis
B0030163biological_processprotein catabolic process
B0031667biological_processresponse to nutrient levels
B0042277molecular_functionpeptide binding
B0042470cellular_componentmelanosome
B0098830cellular_componentpresynaptic endosome
B0098982cellular_componentGABA-ergic synapse
B0099532biological_processsynaptic vesicle endosomal processing
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNLWV
ChainResidueDetails
AVAL30-VAL41
AALA223-GLY234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24090084","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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