‹ ›
MYP_084648
← PREVIOUS NEXT → BACK
Basic Information
Unnamed
Antimicrobial
Antiviral
Antiviral ▸ Anti-HIV ▸ Anti-HIV-1
Antiviral ▸ Antiviral mechanism ▸ Viral replication inhibition
Enzyme modulation ▸ Enzyme inhibition ▸ Integrase inhibition
Standard
6 amino acids
C34H55N11O7
Standard
Sequence
KLAGRW
Physicochemical Analysis
729.87 Da
11.00
1.76
1.55
0.2932
-0.68
0.77
-0.18
89.65
81.67
0.1667
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
312.53
-1.36
12.0
9.0
23.0
52.0
2.0
5.0
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_0032692 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antiviral
PaperHIPdb: a database of experimentally validated HIV inhibiting peptides PMID23359817 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/23359817/
RECORD: Rec_0090580 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antiviral Replication inhibition
inhibition of strand transfer catalyzed by integrase
100 μM
IC50
Mammalian: 1.3 h; Yeast: 3 min; E. coli: 2 min
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. | Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. | J Med Chem. 2006 Jul 27;49(15):4477-86. | DOI:10.1021/jm060307u | PMID:16854053 PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
RECORD: Rec_0148740 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial Antiviral
HIV-1:Inhibition of 3′-processing catalyzed by integrase
100 μM
IC50
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
RECORD: Rec_0230492 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial Antiviral
inhibition of strand transfer catalyzed by integrase
100 μM
IC50
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
RECORD: Rec_0286267 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Protein-derived synthetic peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antiviral Anti-HIV-1 Replication inhibition
HIV-1
100 μM
IC50
Mammalian: 1.3 h; Yeast: 3 min; E. coli: 2 min
PaperSequence-based design and discovery of peptide inhibitors of HIV-1 integrase: insight into the binding mode of the enzyme. | Li HY, Zawahir Z, Song LD, Long YQ, Neamati N. | J Med Chem. 2006 Jul 27;49(15):4477-86. | DOI:10.1021/jm060307u | PMID:16854053 PMID16854053 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16854053/
1 2 NEXT LAST
Showing 5 records on this page · Page 1 of 2