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MYP_072486
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Basic Information
EeCentrocin 2
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
32 amino acids
C156H246N52O38S
Standard
Sequence
WGHKLRSSWNKVKHAVKKGAGYASGACRVLGH
Physicochemical Analysis
3490.01 Da
10.67
7.01
6.63
0.2189
-0.60
0.61
-0.08
54.28
64.06
0.0938
12490.00
12490.00
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
1460.95
-15.03
55.0
49.0
116.0
247.0
8.0
32.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0168583 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Pyroglutamylation
Amidation
Chain A (shown) is connected with chain B (EVGKYCAVAHAIH, amidated) via a disulfide bond. In chain B, the N-terminal Q is pyroglutamic acid (Glp). Trp is bromated at position 6 (6-bromotryptophan). Sequence analysis: APD analysis reveals that the sequence of chain A shows 46.8% similarity to EeCentrocin 1
Bio-Activity Profile
Antimicrobial Antifungal
Escherichia coli
1.56-6.25 μM
MIC
PaperNovel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational Modifications.
RECORD: Rec_0184233 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Pyroglutamylation
Amidation
Chain A (shown) is connected with chain B (EVGKYCAVAHAIH, amidated) via a disulfide bond. In chain B, the N-terminal Q is pyroglutamic acid (Glp). Trp is bromated at position 6 (6-bromotryptophan). Sequence analysis: APD analysis reveals that the sequence of chain A shows 46.8% similarity to EeCentrocin 1
Bio-Activity Profile
Antimicrobial Antifungal
Corynebacterium glutamicum
0.78 μM
MIC
PaperNovel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational Modifications.
RECORD: Rec_0188201 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Pyroglutamylation
Amidation
Chain A (shown) is connected with chain B (EVGKYCAVAHAIH, amidated) via a disulfide bond. In chain B, the N-terminal Q is pyroglutamic acid (Glp). Trp is bromated at position 6 (6-bromotryptophan). Sequence analysis: APD analysis reveals that the sequence of chain A shows 46.8% similarity to EeCentrocin 1
Bio-Activity Profile
Antimicrobial Antifungal
Candida albicans
50 μM
MIC
PaperNovel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational Modifications.
RECORD: Rec_0194897 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Pyroglutamylation
Amidation
Chain A (shown) is connected with chain B (EVGKYCAVAHAIH, amidated) via a disulfide bond. In chain B, the N-terminal Q is pyroglutamic acid (Glp). Trp is bromated at position 6 (6-bromotryptophan). Sequence analysis: APD analysis reveals that the sequence of chain A shows 46.8% similarity to EeCentrocin 1
Bio-Activity Profile
Antimicrobial Antifungal
A. pullulans
25 μM
MIC
PaperNovel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational Modifications.
RECORD: Rec_0223128 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Saccharomyces cerevisiae
12.5 μM
MIC
PMID27007817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27007817/
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