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7AGC

Protease Sapp1p from Candida parapsilosis in complex with KB74

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
D0004190molecular_functionaspartic-type endopeptidase activity
D0005576cellular_componentextracellular region
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0016787molecular_functionhydrolase activity
F0004190molecular_functionaspartic-type endopeptidase activity
F0005576cellular_componentextracellular region
F0006508biological_processproteolysis
F0008233molecular_functionpeptidase activity
F0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIIDTGSSDFWV
ChainResidueDetails
AVAL29-VAL40
AALA217-PHE228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP220
BASP32
BASP220
DASP32
DASP220
FASP32
FASP220

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PDB entries from 2025-06-18

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