PPIRE12053

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 Peptide432-446
Peptide_Sequence TNLKLKKIYFYWLCR
Peptide_Length 15
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)[C@@H](C)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)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 1989.45
Aliphatic_Index 104.00000
Aromaticity 0.26667
Average_Rotatable_Bonds 4.33333
Charge_at_pH_7 3.93342
Isoelectric_Point 10.33328
Number_of_Hydrogen_Bond_Acceptors 25
Number_of_Hydrogen_Bond_Donors 28
Topological_Polar_Surface_Area 730.25000
X_logP_energy -0.93053
Interaction Information
Affinity IC50=5.18 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