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 FormulaC895H1423N257O274S10

DescriptionStandard

        MSAIRQSMIYCSVAAVIGIVTTVYPNDLQTSRAGLELIASYENCVSCTYKDSIGKNTIGIGSTRGLDGKPVPNNQLLSNDDIARLLVRDIKESEECVIKYFNGQKMPQPVFDSVVSLVYNNGCYGTRWNKSANRPTFISRYAVSGDWNNVCYRFSDFVNAGGVRSKGLVNRRTAEQKLCLQYRQ
    

Molecular Weight20488.08 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-0.27

Hydrophobic Moment 0.85

Boman Index-0.03

Instability Index47.90

Aliphatic Index 83.10

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 8685.19

LogP -107.28

H-bond Donors 310.0

H-bond Acceptors 291.0

Rotatable Bonds 680.0

Heavy Atoms 1436.0

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_0124170 VERIFIED: NO

Provenance & Taxonomy

OrganismYersinia phage phi80-18 [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