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MYP_110469
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Basic Information
G19Q (truncated isoform of thanatin, residue 1-19)
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Standard
19 amino acids
C92H158N30O25S2
Standard
Sequence
GSKKPVPIIYCNRRTGKCQ
Physicochemical Analysis
2148.55 Da
10.06
4.74
4.50
0.2493
-0.86
0.49
-0.29
43.02
56.32
0.0526
1490.00
1615.00
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
918.27
-10.62
34.0
32.0
71.0
149.0
3.0
20.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0088757 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
11-18
APD analysis reveals that this sequence is similar (90.48%) to Thanatin K: 16%, I=C=G=P=R: 11%. Chemical modification: C-C disulfide bond
Bio-Activity Profile
Antimicrobial Antifungal
P-aeruginosa
>40 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
RECORD: Rec_0090503 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Antifungal
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. doi: 10.1073/pnas.93.3.1221. PMID: 8577744. PMID8577744 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8577744/
RECORD: Rec_0097408 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
11-18
APD analysis reveals that this sequence is similar (90.48%) to Thanatin K: 16%, I=C=G=P=R: 11%. Chemical modification: C-C disulfide bond
Bio-Activity Profile
Antimicrobial Antifungal
A. pisi
20-40 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
RECORD: Rec_0105857 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Thanatin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
11-18
APD analysis reveals that this sequence is similar (90.48%) to Thanatin K: 16%, I=C=G=P=R: 11%. Chemical modification: C-C disulfide bond
Bio-Activity Profile
Antimicrobial Antifungal
B. megaterium
5-10 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
RECORD: Rec_0120054 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Antifungal
Trichoderma viride
10-20 μM
MIC
PaperStructure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1221-1225. doi: 10.1073/pnas.93.3.1221. PMID: 8577744. PMID8577744 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/8577744/
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