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_5607
Peptide NameLEA1_PHAVU
PMID(s)--NA--
Plant Source (Scientific Name)Phaseolus vulgaris
Plant Source (Common Name)Kidney bean
Plant FamilyFabaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function Description3D-structure; Alpha-amylase inhibitor; Direct protein sequencing; Glycoprotein; Lectin; Signal | Alpha-amylase inhibitor 1 precursor (Alpha-AI-1) (Alpha-AI1) (Lectin),[Contains: Alpha-amylase inhibitor 1 chain 1; Alpha-amylase inhibitor,1 chain 2].
Activity Against--NA--
IC50 value--NA--
SequenceGFSATSGAYQWSYETHDVLSWSFSSKFINLKDQKSERSNIVLNKILGNLQLSYNSYDSMSRAFYSAPIQIRDSTTGNVASFDTNFTMNIRTHRQANMIMASSKLLSLALFLALLSHANSATETSFIIDAFNKTNLILQGDATVSSNSAVGLDFVLVPVQPESKGDTVTVEFDTFLSRISIDVNNNDIKSVPWDVHDYDGQNAEVRITYNSSTKVFSVSLSNPSTGKSNNVSTTVELEKEVYDWVSV
Sequence Length246
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)27207.22
Monoisotopic Molecular Weight (Da)27190.49
Isoelectric Point (pI)5.03
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_5607


External links (Uniprot, PDB and Source Information Database)
UniprotP02873
NCBI--NA--
EMBLJ01261
Link to Source DatabasesSPdb137462
Addtional InformationFUNCTION:Lectin and alpha-amylase inhibitor. Act as a defensive protein against insects.SUBUNIT:Heterodimer of chain 1 and chain 2.PTM:Proteolytic processing yields active form.SIMILARITY:Belongs to the leguminous lectin family.