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 Length184 amino acids

Chemical FormulaC893H1419N257O272S10

DescriptionStandard

        MSAIRQSMIYCSVAAVIGIVTTVYPNDLQTSRAGLELIASYENCVSCTYKDSIGKNTIGIGSTRGLDGKPVPNNQLLSNDDIARLLVRDIKESEECVIKYFNGQKMPQPVFDSAVSLVYNNGCYGTRWNKSANRPTFIARYAVAGDWNNVCYRFSDFVNAGGVRSKGLVNRRTAEQKLCIQYRQ
    

Molecular Weight20428.03 Da

Isoelectric Point (pI)9.10

Net Charge (pH 7.0)6.44

Net Charge (pH 7.4) 6.08

Charge Density (pH 7.0) 0.0350

GRAVY Index-0.25

Hydrophobic Moment 0.85

Boman Index-0.02

Instability Index44.04

Aliphatic Index 83.15

Aromaticity 0.0924

Extinction Coeff. Reduced 25900.00

Extinction Coeff. Oxidized 26275.00

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

Amino Acid Composition

TPSA 8644.73

LogP -105.62

H-bond Donors 308.0

H-bond Acceptors 289.0

Rotatable Bonds 677.0

Heavy Atoms 1432.0

Ring Count 25.0

Amide Bonds 206.0

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_0166099 VERIFIED: NO

Provenance & Taxonomy

OrganismYersinia phage fHe-Yen3-01 [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