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3TNE

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE RIT A 401
ChainResidue
AILE30
AASN125
AASP220
AGLY222
ATHR223
ATHR224
ATYR227
AILE303
AASP32
AGLY34
AARG77
ATYR78
AGLY79
AASP80
ASER82
AASP114

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE RIT B 401
ChainResidue
BILE30
BASP32
BGLY34
BARG77
BTYR78
BGLY79
BASP80
BSER82
BVAL113
BASP114
BASN125
BASP220
BGLY222
BTHR223
BTHR224
BILE303

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 Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP220
BASP32
BASP220

221051

PDB entries from 2024-06-12

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