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MYP_135131
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Basic Information
Esculentin-1B
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Hormonal / Endocrine ▸ Hormone peptide
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Toxicity / Safety ▸ Negative safety assay result ▸ Non-hemolytic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
46 amino acids
C212H371N59O60S3
Standard
Sequence
GIFSKLAGKKLKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC
Physicochemical Analysis
4802.77 Da
9.63
4.74
4.49
0.1030
0.20
0.59
0.09
-8.14
114.35
0.0217
0.00
125.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
1938.95
-17.66
69.0
68.0
175.0
334.0
1.0
47.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0294267 VERIFIED: YES
Provenance & Taxonomy
Pelophylax esculentus [Animal]
Esculentin
Structure & Mods
Linear peptide with a single intramolecular disulfide-stabilized loop [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
40-46
Bio-Activity Profile
Antimicrobial Antibacterial
PaperT. Chen et al. / Genomics 87 (2006) 638-644. Cloning from tissue surrogates: Antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs Evidence URLhttps://www.uniprot.org/uniprotkb/P40844/entry
RECORD: Rec_0362801 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Brevinin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial
PaperSimmaco M., Mignogna G., Barra D., Bossa F.;. "Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides."; J. Biol. Chem. 269:11956-11961). Evidence URLhttps://www.uniprot.org/uniprotkb/ES1B_RANES/entry
RECORD: Rec_0379244 VERIFIED: NO
Provenance & Taxonomy
Rana saharica [Animal]
Esculentin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
PaperEsculentin-1B Evidence URLhttps://www.uniprot.org/uniprotkb/P84841/entry
RECORD: Rec_0385895 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct based on Rana esculenta [Synthetic]
Esculentin
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
40-46
Bio-Activity Profile
Antimicrobial
Escherichia coli D21
0.2 μM
MIC
PaperAntimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.
RECORD: Rec_0390079 VERIFIED: YES
Provenance & Taxonomy
Rana ridibunda [Animal]
Esculentin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Hemolytic
shows hemolytic activity
Hemolysis
Evidence URLhttps://camp.bicnirrh.res.in/seqDisp.php?id=CAMPSQ1791
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