PPepDB-ID	"Peptide Name"	PMID	"Plant source"	"Plant Family"	"Peptide Family"	"Peptide function"	"Peptide function description"	"Activity against"	Sequence	"Sequence Length"	Validation	"Avg. Molecular wt(Da)"	"Monoisotopic molecular wt(Da)"	pI	Method	"Additional information"
PPepDB_3968	"Pa-AMP1 (PAFP-S)"	"10759497, 10082954"	"Phytolacca americana"	Phytolaccaceae	Knottin	"Antibacterial, Antifungal"	"possesses antifungal activity; Target site- Lipid Bilayer"	"Gram-positive bacteria: Bacillus megaterium (IC50= 8 µg/mL), Staphyanococcus sp. (IC50= 11 µg/mL). NOTE! not active against Escherichia coli. Fungi: Alternaria panax, Fusarium sp., Rhizoctonia solani."	AGCIKNGGRCNASAGPPYCCSSYCFQIAGQSYGVCKNR	38	"Experimental evidence at protein level"	3935.47	3932.71	8.9	NMR	"It contains three disulfide bonds: 3,20; 10,24; 19,35.The global fold involves a cystine-knotted three-stranded antiparallel beta-sheet (residues 8-10, 23-27, 32-36), a flexible loop (residues 14-19), and four beta-reverse turns (residues 4-8, 11-14, 19-22, 28-32). This structure features all the characteristics of the knottin fold. It is the first structural model of an antifungal peptide that adopts a knottin-type structure (Gao et al., 2001). You can rotate, zoom, and view the 3D structure here in the PDB . A hydrophobic surface, comprising Y23, F25, I27, Y32, and V34, is bordered by basic R9, K36, and R38. Such a structural feature may be important for antimicrobial activity. Updated 11/2011; 2/2014; 8/2015 GW."