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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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP218

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0CY29
ChainResidueDetails
AASP32
AGLY85
AASP191
AASP214
AASP218

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN257
AASN265

218853

PDB entries from 2024-04-24

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