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MYP_150341
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Basic Information
HG34
Antimicrobial
Standard
19 amino acids
C96H159N29O21S
Standard
Sequence
KWKKALLHHGLNCAKGVLA
Physicochemical Analysis
2087.54 Da
10.04
3.92
3.60
0.2063
0.01
0.42
0.09
-1.97
113.16
0.0526
5500.00
5500.00
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
807.44
-4.74
29.0
28.0
71.0
147.0
4.0
19.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0002141 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Halocidin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
APD analysis reveals that this sequence is 89.47% similar to HG1 L=K: 21%, A: 16%, G=H: 11%. A lysine is added to the N-terminus of the wild type sequence. Warning: chain B sequence is the same as chain A. Chemical modification: there is an intermolecular S-S bond between the two chains
Bio-Activity Profile
Antimicrobial
Bacillus subtilis
2 μg/mL
MIC
PaperAntimicrobial activity of a halocidin-derived peptide resistant to attacks by proteases.
RECORD: Rec_0039250 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Halocidin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
APD analysis reveals that this sequence is 89.47% similar to HG1 L=K: 21%, A: 16%, G=H: 11%. A lysine is added to the N-terminus of the wild type sequence. Warning: chain B sequence is the same as chain A. Chemical modification: there is an intermolecular S-S bond between the two chains
Bio-Activity Profile
Antimicrobial
C. freundii
4 μg/mL
MIC
PaperAntimicrobial activity of a halocidin-derived peptide resistant to attacks by proteases.
RECORD: Rec_0094081 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Halocidin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
APD analysis reveals that this sequence is 89.47% similar to HG1 L=K: 21%, A: 16%, G=H: 11%. A lysine is added to the N-terminus of the wild type sequence. Warning: chain B sequence is the same as chain A. Chemical modification: there is an intermolecular S-S bond between the two chains
Bio-Activity Profile
Antimicrobial
Pseudomonas aeruginosa MDRPA
4 μg/mL
MIC
PaperAntimicrobial activity of a halocidin-derived peptide resistant to attacks by proteases.
RECORD: Rec_0100671 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Halocidin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
APD analysis reveals that this sequence is 89.47% similar to HG1 L=K: 21%, A: 16%, G=H: 11%. A lysine is added to the N-terminus of the wild type sequence. Warning: chain B sequence is the same as chain A. Chemical modification: there is an intermolecular S-S bond between the two chains
Bio-Activity Profile
Antimicrobial
K. oxytoca
2 μg/mL
MIC
PaperAntimicrobial activity of a halocidin-derived peptide resistant to attacks by proteases.
RECORD: Rec_0135957 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Halocidin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
APD analysis reveals that this sequence is 89.47% similar to HG1 L=K: 21%, A: 16%, G=H: 11%. A lysine is added to the N-terminus of the wild type sequence. Warning: chain B sequence is the same as chain A. Chemical modification: there is an intermolecular S-S bond between the two chains
Bio-Activity Profile
Antimicrobial
Micrococcus luteus
4 μg/mL
MIC
PaperAntimicrobial activity of a halocidin-derived peptide resistant to attacks by proteases.
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