Peptide Database

Peptide NameEndolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase)

Function Ontology

Antimicrobial

Antimicrobial ▸ Antibacterial ▸ Bacteriolytic activity ▸ Bacteriolytic enzyme

Enzyme / Catalytic activity ▸ Hydrolase

Enzyme / Catalytic activity ▸ Hydrolase ▸ Glycosidase

Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity

Toxicity / Safety ▸ Negative safety assay result ▸ Non-hemolytic

Standard StatusStandard

Sequence Length323 amino acids

Chemical FormulaC1645H2584N452O479S21

DescriptionStandard

        MKTLSAGIIFMTEDKDLFMGRVTGSRKTGMMAHRWDIPKGRVENSDLSALDAARRECLEETGFGNYNPDLLEDLGVFKYSSNKDLQLFYYTIPVEHEMFRNCRCESYFENKDGVMIPEMDAFALIPRTQWQYVMGPSLYRIMNNLFNFINTFYKYLGGIMNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLSVAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVIATFRTGTCDAYKNL
    

Molecular Weight37030.22 Da

Isoelectric Point (pI)8.74

Net Charge (pH 7.0)4.74

Net Charge (pH 7.4) 4.19

Charge Density (pH 7.0) 0.0147

GRAVY Index-0.34

Hydrophobic Moment 0.77

Boman Index-0.03

Instability Index36.59

Aliphatic Index 80.34

Aromaticity 0.1084

Extinction Coeff. Reduced 44350.00

Extinction Coeff. Oxidized 44725.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

3D PDB MODEL

Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.

2D CHEMICAL STRUCTURE

Drag to move

Drag to move. Use the buttons to zoom.

RECORD: Rec_0186395 VERIFIED: NO

Provenance & Taxonomy

OrganismEscherichia phage T2 [Virus]

FamilyGlycosyl hydrolase 24

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase Cytolytic Non-hemolytic