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 IDPPepDB_2099
Peptide NameTu-AMP2 alpha chain
PMID(s)15056889
Plant Source (Scientific Name)Tulipa gesneriana
Plant Source (Common Name)Garden tulip
Plant FamilyLiliaceae
Peptide FamilyThionin
Peptide FunctionAntibacterial, Antifungal
Peptide Function DescriptionTarget site- Lipid Bilayer; Shows high antimicrobial activity by binding to chitin in a reversible way.
Activity AgainstErwinia carotovora subsp. carotovora (IC50: 15 µg/ml), Agrobacterium radiobacter (IC50: 17 µg/ml), Agrobacterium rhizogenes (IC50: 20 µg/ml), Clavibacter michiganensis subsp. michiganensis (IC50: 17 µg/ml), Curtobacterium flaccumfaciens pv. oortii (IC50: 15 µg/ml), Fusarium oxysporum (IC50: 2 µg/ml), Geotrichum candidum(IC50: 2 µg/ml)
IC50 value15 µg/ml | 17 µg/ml | 20 µg/ml | 17 µg/ml | 15 µg/ml | 2 µg/ml | 2 µg/ml
SequenceKSCCRNTTARNCYNVCRIPG
Sequence Length20
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)2259.62
Monoisotopic Molecular Weight (Da)2258.03
Isoelectric Point (pI)9.3
Method / ExtractionRP-HPLC


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_2099


External links (Uniprot, PDB and Source Information Database)
Uniprot--NA--
NCBI--NA--
EMBL--NA--
Link to Source DatabasesDB8276, CAMPSQ2796, APD_00534
Addtional InformationSynthesis Type: Ribosomal; This peptide is a part of Dimer; It is a unique heterodimer linked by four pairs of disulfide bonds. Shown is the sequence for chain A. The sequence for chain B is TPRPVCAATCDCKIITGTKCPPGYEK. It has chitin-binding activity.