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MYP_164546
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Basic Information
Ranacyclin-B-RL1
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Enzyme modulation ▸ Enzyme inhibition ▸ Trypsin inhibitor
Standard
20 amino acids
C96H160N30O23S2
Standard
Sequence
AALRGCWTKSIPPKPCPGKR
Physicochemical Analysis
2166.61 Da
10.33
4.77
4.55
0.2387
-0.67
0.28
-0.16
41.55
49.00
0.0500
5500.00
5625.00
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
839.17
-8.10
31.0
30.0
65.0
151.0
6.0
19.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0210980 VERIFIED: YES
Provenance & Taxonomy
Odorrana livida [Animal]
Lividin
Structure & Mods
Linear peptide with a single intramolecular disulfide-stabilized loop [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
6-16
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-negative
Escherichia coli
46.2 μM
MIC
PaperX. Yan et al. / Amino Acids (2011) DOI 10.1007/s00726-011-1079-8. Bi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensivemolecules in Ranidae amphibian skins Evidence URLhttps://www.uniprot.org/uniprotkb/C3RSZ6/entry
RECORD: Rec_0213974 VERIFIED: YES
Provenance & Taxonomy
Odorrana livida [Animal]
Ranacyclin
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Bacillus subtilis ATCC 6633
46.2 μM
MIC
PMID21927839 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/21927839/
RECORD: Rec_0237077 VERIFIED: YES
Provenance & Taxonomy
Odorrana livida [Animal]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
6-16
Bio-Activity Profile
Antimicrobial Antifungal
Staphylococcus aureus
5.8 μM
MIC
PaperBi-functional peptides with both trypsin-inhibitory and antimicrobial activities are frequent defensive molecules in Ranidae amphibian skins
RECORD: Rec_0300462 VERIFIED: YES
Provenance & Taxonomy
Odorrana livida [Animal]
Structure & Mods
disulfide-constrained cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
None
6-16
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
Staphylococcus aureus
5.8 μM
MIC
PMID21927839 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/21927839/
RECORD: Rec_0327879 VERIFIED: NO
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antibacterial Antimicrobial Antifungal Anti-Gram-positive Anti-Gram-negative
PaperCAMP: Collection of sequences and structures of antimicrobial peptides PMID24265220 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/24265220/
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