‹ ›
MYP_093826
← PREVIOUS NEXT → BACK
Basic Information
2K4L_W10
Antimicrobial
Standard
13 amino acids
C86H146N18O14
Standard
Sequence
IILLLLKKFWKKL
Physicochemical Analysis
1656.19 Da
10.48
3.76
3.55
0.2889
1.10
0.59
0.31
10.98
210.00
0.1538
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
532.39
4.02
19.0
18.0
59.0
118.0
3.0
12.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0001797 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (92.31%) to Temporin-1CEc analog 2K4L L: 38%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. faecium
3.13 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0009401 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (92.31%) to Temporin-1CEc analog 2K4L L: 38%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
B. cereus
6.25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0101498 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (92.31%) to Temporin-1CEc analog 2K4L L: 38%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. cloacae
6.25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0150507 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (92.31%) to Temporin-1CEc analog 2K4L L: 38%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Escherichia coli
3.13 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0217111 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (92.31%) to Temporin-1CEc analog 2K4L L: 38%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. aerogenes
3.13 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
1 2 NEXT LAST
Showing 5 records on this page · Page 1 of 2