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MYP_123948
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Basic Information
EeCentrocin 1 Chain A
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Standard
30 amino acids
C143H228N50O36S
Standard
Sequence
GWWRRTVDKVRNAGRKVAGFASKACGALGH
Physicochemical Analysis
3255.72 Da
11.57
5.84
5.56
0.1945
-0.48
0.77
-0.13
35.30
58.67
0.1000
11000.00
11000.00
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
1413.99
-15.52
54.0
44.0
107.0
230.0
6.0
30.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0231756 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
Chain A (shown) is connected with chain B (DIGKYCGYAHALN, amidated) via a disulfide bond. Trp is bromated at position 6 (6-bromotryptophan). Sequence analysis:APD analysis reveals that the sequence of chain A shows 45% similarity to Centrocin 2
Bio-Activity Profile
Antimicrobial Antifungal
planktonic 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_0236256 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
Pseudomonas aeruginosa ATCC 15692
PMID27007817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27007817/
RECORD: Rec_0242223 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
Escherichia coli NR 698
1.56 μM
MIC
PMID27007817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27007817/
RECORD: Rec_0260250 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
A. pullulans
12.5 μM
MIC
PMID27007817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27007817/
RECORD: Rec_0274274 VERIFIED: YES
Provenance & Taxonomy
Echinus esculentus [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
Chain A (shown) is connected with chain B (DIGKYCGYAHALN, amidated) via a disulfide bond. Trp is bromated at position 6 (6-bromotryptophan). Sequence analysis:APD analysis reveals that the sequence of chain A shows 45% similarity to Centrocin 2
Bio-Activity Profile
Antimicrobial Antifungal
Escherichia coli #1
0.1 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.
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