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3Q70

Secreted aspartic protease in complex with ritonavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE RIT A 2001
ChainResidue
AASP32
AASP218
AGLY220
ATHR221
ATHR222
ATYR225
AILE305
AHOH6004
AHOH6106
AHOH6173
AGLY34
ASER35
AGLY83
ATYR84
AGLY85
AILE119
AASP120
AASN131

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3000
ChainResidue
AASP57
AGLU324
AHOH6195
AHOH6204

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 3001
ChainResidue
AHOH6196
AHOH6199
AHOH6200
AHOH6201
AHOH6202

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MRD A 4001
ChainResidue
ALEU183
ASER326
AHOH6024
AHOH6058
AHOH6137

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIVDTGSSDLWV
ChainResidueDetails
AVAL29-VAL40
AVAL215-LEU226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0CY29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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