Detailed Peptide Information

This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking

Primary Information
PPepDB ID	PPepDB_3972
Peptide Name	Rs-AFP1
PMID(s)	1639777, 7780308, 9636715, 8422949, 25153857, 16653017
Plant Source (Scientific Name)	Raphanus sativus
Plant Source (Common Name)	Radish
Plant Family	Brassicaceae
Peptide Family	Defensin
Peptide Function	Antifungal
Peptide Function Description	Exhibit potent antifungal activity in vitro.
Activity Against	Fungi: Alternaria brassicola (IC50= 15 µg/mL), Botrytis cinerea (IC50= 8 µg/mL), Fusarium culmorum (IC50= 5 µg/mL), Fusarium oxysporum (IC50= 30 µg/mL), Pyricularia oryzae (IC50= 0.3 µg/mL), Verticiliium dahliae (IC50= 5 µg/mL). NOTE! Not tested against bacteria.
IC50 value	15 µg/mL | 8 µg/mL | 5 µg/mL | 30 µg/mL | 0.3 µg/mL | 5 µg/mL
Sequence	QKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC
Sequence Length	51
Validation	Experimental evidence at protein level
Average Molecular Weight (Da)	5694.55
Monoisotopic Molecular Weight (Da)	5690.56
Isoelectric Point (pI)	8.72
Method / Extraction	NMR

Secondary Information
Tertiary Structure and DSSP Report	Click to View Structure
Physico-Chemical Properties of peptides	Click to View Physico-Chemical Details of PPepDB_3972

External links (Uniprot, PDB and Source Information Database)
Uniprot	P69241, P30227, P30231, P69240
NCBI	1703204
EMBL	--NA--
Link to Source Databases	PhytAMP_PHYT00052, DEFENSINS-Knowledgebase_241, CAMPSQ917, CAMPSQ1033, APD_00286
Addtional Information	Signal peptide: 1-29; Mature peptide: 30-80; Activity of Rs-AFP1 to Rs-AFP3 reduced in the presence of metal ions. Note that in the structure determined by NMR, the first residue of the peptide sequence is Glu rather than Gln.You can rotate, zoom, and view the 3D structure here in the PDB . Updated 2/2014.