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_4805
Peptide NameLECC_PHYAM
PMID(s)--NA--
Plant Source (Scientific Name)Phytolacca americana
Plant Source (Common Name)Virginian pokeweed
Plant FamilyPhytolaccaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function Description3D-structure; Chitin-binding; Direct protein sequencing; Lectin; Mitogen; Repeat; Signal | Lectin-C precursor (PL-C).
Activity Against--NA--
IC50 value--NA--
SequenceCGLTDDHCEDGCQSQCDLPTLLPSPLRRIIAIRKLKANLANMLSELCCSQYGWCGNSDGHCGEGCQSQCSYWRCGKDFGGRLCTEDMCCSQYGWMKRSNSIAVMLVLVLSSLMLLLPVEGQGHEGHGVGEILLMGKLGAPVCGVRASGRVCPDGYCCSQWGYCGTTEEYCGKGCQSQCDYNRCGKEFGGKECHD
Sequence Length194
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)21042.08
Monoisotopic Molecular Weight (Da)21027.38
Isoelectric Point (pI)5.71
Method / Extraction--NA--


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_4805


External links (Uniprot, PDB and Source Information Database)
UniprotQ9AYP9
NCBI--NA--
EMBLAB052963
Link to Source DatabasesSPdb137568
Addtional InformationFUNCTION:N-acetyl-D-glucosamine binding lectin. Almost no hemagglutinating activity towards human erythrocytes. Low mitogenic activity towards human peripheral blood lymphocytes.SUBUNIT:Homodimer. The homodimers are asymmetric; formed in a 'head-to-tail' fashion via hydrophobic interactions between aromatic residues of the carbohydrate-binding sites of each subunit.SIMILARITY:Contains 3 chitin-binding type-1 domains.