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MYP_049425
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Basic Information
Esculentin-2B
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity
Standard
37 amino acids
C169H289N45O44S2
Standard
Sequence
GIFSLVKGAAKLAGKGLAKEGGKFGLELIACKIAKQC
Physicochemical Analysis
3719.51 Da
9.70
4.74
4.49
0.1281
0.45
0.56
0.20
10.16
108.38
0.0541
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
1430.98
-11.35
51.0
51.0
134.0
260.0
2.0
37.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0188028 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial
PaperAPD2: the updated antimicrobial peptide database and its application in peptide design PMID18957441 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18957441/
RECORD: Rec_0205204 VERIFIED: YES
Provenance & Taxonomy
Rana esculenta [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 Antibacterial Anti-Gram-positive Anti-Gram-negative
PMID8163497 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8163497/
RECORD: Rec_0253980 VERIFIED: NO
Provenance & Taxonomy
Rana esculenta [Animal]
Esculentin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
31-37
Bio-Activity Profile
Antimicrobial
PaperAntimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.
RECORD: Rec_0323906 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]
31-37
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/P40846/entry
RECORD: Rec_0410120 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/ES2B_RANES/entry
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