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MYP_165622
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Basic Information
Esculentin-1A
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antibiotic activity
Antimicrobial ▸ Antifungal
Immunology ▸ Innate immune defense ▸ Host defense peptide ▸ Host defense activity
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Standard
46 amino acids
C212H371N59O60S3
Standard
Sequence
GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVRTGIDIAGCKIKGEC
Physicochemical Analysis
4802.77 Da
9.63
4.74
4.49
0.1030
0.22
0.59
0.10
-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_0160450 VERIFIED: YES
Provenance & Taxonomy
Pelophylax lessonae [Animal]
Esculentin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
40-46
Bio-Activity Profile
Antimicrobial Antifungal
Staphylococcus aureus Cowan I
0.4 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_0165000 VERIFIED: YES
Provenance & Taxonomy
Pelophylax fukienensis [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 Anti-Gram-negative
Escherichia coli
2.8 μM
MIC
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/Q1MU23/entry
RECORD: Rec_0172013 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 Anti-Gram-negative
Escherichia coli
2.8 μM
MIC
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/P40843/entry
RECORD: Rec_0192215 VERIFIED: NO
Provenance & Taxonomy
Rana fukienensis [Animal]
Esculentin
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
PMID16427248 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16427248/
RECORD: Rec_0197286 VERIFIED: YES
Provenance & Taxonomy
Pelophylax lessonae [Animal]
Esculentin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
40-46
Bio-Activity Profile
Antimicrobial Antifungal
Pseudomonas aeruginosa ATCC 15692
0.7 μM
MIC
PaperAntimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.
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