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_5889
Peptide NameFKB21_ARATH
PMID(s)--NA--
Plant Source (Scientific Name)Arabidopsis thaliana
Plant Source (Common Name)Mouse-ear cress
Plant FamilyBrassicaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function DescriptionComplete proteome; Endoplasmic reticulum; Isomerase; Rotamase; Signal | FK506-binding protein 2-1 precursor (EC 5.2.1.8) (Peptidyl-prolyl cis-,trans isomerase) (PPIase) (Rotamase) (15 kDa FKBP) (FKBP-15-1).Endoplasmic reticulum lumen (Potential).
Activity Against--NA--
IC50 value--NA--
SequenceKGDKIKVHYRGKLTDGTVFDSSFERGDPIEFELGTGQVIPGWDQGLLGACMMSSASAMKAVGFLLLLTILTLAYAKKSGDVTELQIGVKYKPQKCDLQAHNELVGEKRKLKIPSKLGYGDNGSPPKIPGGATLIFDTELVAVNGEPSSEAKSK
Sequence Length153
ValidationExperimental evidence at transcript level
Average Molecular Weight (Da)16354.86
Monoisotopic Molecular Weight (Da)16344.56
Isoelectric Point (pI)8.49
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_5889


External links (Uniprot, PDB and Source Information Database)
UniprotQ38935
NCBI--NA--
EMBLU52046
Link to Source DatabasesSPdb83538
Addtional InformationFUNCTION:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.CATALYTIC ACTIVITY:Peptidylproline (omega=180) = peptidylproline (omega=0).SIMILARITY:Belongs to the FKBP-type PPIase family. FKBP2 subfamily.SIMILARITY:Contains 1 PPIase FKBP-type domain.