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2H6T

Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 602
ChainResidue
AHIS131
AASP191
AHIS197
AASP214

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR CHAIN B OF PEPSTATIN A
ChainResidue
ATYR84
AGLY85
AASP86
AASP218
AGLY220
ATHR221
ATHR222
ATYR303
AHOH2005
AHOH2212
BHOH2106
BHOH2147
BHOH2218
BHOH2319
AVAL12
AASP32
AGLY34
ASER35
AGLU83

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

site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. LTVVIDT
ChainResidueDetails
ALEU27-THR33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues312
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues15
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17510964","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H6T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PDB","id":"2H6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H6T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP32

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP218

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR221
ASER35
AASP218
AASP32

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
AASP218
AASP32
ATHR33
ASER219

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ASER35
AASP218
AASP32

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ASER35
ATYR84
AASP218
AASP32

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ATHR221
AASP218
AASP32
ATHR33

243083

PDB entries from 2025-10-15

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