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1EAG

Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450

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 Residues20
DetailsBINDING SITE FOR RESIDUE A70 A 343
ChainResidue
ASER88
ASER118
AILE119
AGLU193
ALEU216
AASP218
AGLY220
ATHR221
ATHR222
ATYR225
AASN301
AHOH354
AHOH373
ATHR13
AASP32
AGLY34
AILE82
ATYR84
AGLY85
AASP86

site_idCAT
Number of Residues2
DetailsCATALYTIC SITE
ChainResidue
AASP32
AASP218

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

239492

PDB entries from 2025-07-30

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