PPIRE11999

Target Protein Information
Protein_Name NADPH oxidase 2
Protein_Sequence MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF
Organism_Source Homo sapiens
Functional_Classification oxidoreductases
Cellular_Localization Plasma membrane
Gene_Names CYBB
UniProt_ID P04839
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name Peptide468-482
Peptide_Sequence RNNAGFLSYNIYLTG
Peptide_Length 15
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CCCNC(=N)N)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)NCC(=O)O)[C@@H](C)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Acetyl
C-terminal_Modification amide
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1702.89
Aliphatic_Index 84.66667
Aromaticity 0.20000
Average_Rotatable_Bonds 3.53333
Charge_at_pH_7 0.99628
Isoelectric_Point 9.17163
Number_of_Hydrogen_Bond_Acceptors 24
Number_of_Hydrogen_Bond_Donors 26
Topological_Polar_Surface_Area 742.81000
X_logP_energy -7.99163
Interaction Information
Affinity IC50=6.54 uM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Inhibition of NADPH oxidase activation by peptides mapping within the dehydrogenase region of Nox2-A peptide walking study.
Release_Year 2012
PMID 22184755
DOI 10.1189/jlb.1011507