PPIRE06686

Target Protein Information
Protein_Name Secreted aspartic protease 5
Protein_Sequence MFLKNILSVLAFALLIDAAPVKRSPGFVTLDFNVKRSLVDPDDPTVEAKRSPLFLEFTPSEFPVDETGRDGDVDKRGPVAVTLHNEAITYTADITVGSDNQKLNVIVDTGSSDLWIPDSNVICIPKWRGDKGDFCKSAGSYSPASSRTSQNLNTRFDIKYGDGSYAKGKLYKDTVGIGGVSVRDQLFANVWSTSARKGILGIGFQSGEATEFDYDNLPISLRNQGIIGKAAYSLYLNSAEASTGQIIFGGIDKAKYSGSLVDLPITSEKKLTVGLRSVNVRGRNVDANTNVLLDSGTTISYFTRSIVRNILYAIGAQMKFDSAGNKVYVADCKTSGTIDFQFGNNLKISVPVSEFLFQTYYTSGKPFPKCEVRIRESEDNILGDNFLRSAYVVYNLDDKKISMAPVKYTSESDIVAIN
Organism_Source Candida albicans (strain SC5314 / ATCC MYA-2876)
Functional_Classification aspartic proteases
Cellular_Localization Extracellular
Gene_Names SAP5
UniProt_ID P43094
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name pepstatin A
Peptide_Sequence VVXVXL
Peptide_Length 6
Peptide_SMILES CC(C)C[C@H](NC(=O)CNC(=O)[C@@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)C(C)C)C(=O)O
Chemical_Modification X3=statine; X5=statine
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Acetyl
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 542.68
Aliphatic_Index 210.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 2.66667
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 7
Number_of_Hydrogen_Bond_Donors 7
Topological_Polar_Surface_Area 208.82000
X_logP_energy -0.90080
Interaction Information
Affinity IC50=6 nM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID 2QZX
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title X-ray structures of Sap1 and Sap5: structural comparison of the secreted aspartic proteinases from Candida albicans.
Release_Year 2008
PMID 18384081
DOI 10.1002/prot.22021