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Open data
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Basic information
Entry | Database: PDB / ID: 1wlp | ||||||
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Title | Solution Structure Of The P22Phox-P47Phox Complex | ||||||
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![]() | OXIDOREDUCTASE/Signaling Protein / SH3 domain / polyproline / OXIDOREDUCTASE-Signaling Protein COMPLEX | ||||||
Function / homology | ![]() smooth muscle hypertrophy / reactive oxygen species biosynthetic process / regulation of respiratory burst involved in inflammatory response / positive regulation of toll-like receptor 2 signaling pathway / superoxide-generating NADPH oxidase activator activity / phagolysosome / superoxide-generating NAD(P)H oxidase activity / positive regulation of epidermal growth factor-activated receptor activity / positive regulation of defense response to bacterium / mucus secretion ...smooth muscle hypertrophy / reactive oxygen species biosynthetic process / regulation of respiratory burst involved in inflammatory response / positive regulation of toll-like receptor 2 signaling pathway / superoxide-generating NADPH oxidase activator activity / phagolysosome / superoxide-generating NAD(P)H oxidase activity / positive regulation of epidermal growth factor-activated receptor activity / positive regulation of defense response to bacterium / mucus secretion / Cross-presentation of particulate exogenous antigens (phagosomes) / cytochrome complex assembly / NADPH oxidase complex / respiratory burst / WNT5:FZD7-mediated leishmania damping / cellular response to testosterone stimulus / regulation of release of sequestered calcium ion into cytosol / ROS and RNS production in phagocytes / phosphatidylinositol-3,4-bisphosphate binding / superoxide anion generation / hydrogen peroxide biosynthetic process / protein targeting to membrane / positive regulation of mucus secretion / positive regulation of p38MAPK cascade / positive regulation of reactive oxygen species biosynthetic process / superoxide metabolic process / Detoxification of Reactive Oxygen Species / tertiary granule membrane / RHO GTPases Activate NADPH Oxidases / RAC2 GTPase cycle / RAC3 GTPase cycle / cellular defense response / specific granule membrane / positive regulation of phagocytosis / RAC1 GTPase cycle / cellular response to cadmium ion / phosphatidylinositol binding / secretory granule / establishment of localization in cell / cellular response to glucose stimulus / positive regulation of JNK cascade / cytoplasmic side of plasma membrane / VEGFA-VEGFR2 Pathway / SH3 domain binding / cellular response to reactive oxygen species / phagocytic vesicle membrane / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / oxidoreductase activity / electron transfer activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / endosome / inflammatory response / protein heterodimerization activity / innate immune response / neuronal cell body / dendrite / heme binding / Neutrophil degranulation / endoplasmic reticulum membrane / positive regulation of DNA-templated transcription / membrane / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Ogura, K. / Torikai, S. / Saikawa, K. / Yuzawa, S. / Sumimoto, H. / Inagaki, F. | ||||||
![]() | ![]() Title: NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide Authors: Ogura, K. / Nobuhisa, I. / Yuzawa, S. / Takeya, R. / Torikai, S. / Saikawa, K. / Sumimoto, H. / Inagaki, F. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.4 KB | Display | ![]() |
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PDB format | ![]() | 49.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 246 KB | Display | ![]() |
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Full document | ![]() | 245.8 KB | Display | |
Data in XML | ![]() | 4.9 KB | Display | |
Data in CIF | ![]() | 6.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 2595.971 Da / Num. of mol.: 1 / Fragment: Alpha Polypeptide (1-25) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 15354.016 Da / Num. of mol.: 1 / Fragment: Tandem SH3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz |
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Processing
NMR software | Name: CNS / Classification: refinement |
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Refinement | Software ordinal: 1 / Details: This structure was also refined with ARIA |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 1 |