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- PDB-1oey: Heterodimer of p40phox and p67phox PB1 domains from human NADPH o... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1oey | ||||||
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Title | Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase | ||||||
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![]() | IMMUNE SYSTEM / PB1 HETERODIMER-COMPLEX / NADPH OXIDASE / PB1 DOMAIN / HETERODIMERIZATION | ||||||
Function / homology | ![]() superoxide-generating NADPH oxidase activator activity / phagolysosome / superoxide-generating NAD(P)H oxidase activity / Cross-presentation of particulate exogenous antigens (phagosomes) / NADPH oxidase complex / respiratory burst / phosphatidylinositol-3-phosphate binding / ROS and RNS production in phagocytes / superoxide anion generation / superoxide metabolic process ...superoxide-generating NADPH oxidase activator activity / phagolysosome / superoxide-generating NAD(P)H oxidase activity / Cross-presentation of particulate exogenous antigens (phagosomes) / NADPH oxidase complex / respiratory burst / phosphatidylinositol-3-phosphate binding / ROS and RNS production in phagocytes / superoxide anion generation / superoxide metabolic process / Detoxification of Reactive Oxygen Species / RHO GTPases Activate NADPH Oxidases / RAC2 GTPase cycle / RAC3 GTPase cycle / cellular defense response / phagocytosis / RAC1 GTPase cycle / acrosomal vesicle / small GTPase binding / VEGFA-VEGFR2 Pathway / electron transfer activity / endosome membrane / innate immune response / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wilson, M.I. / Gill, D.J. / Perisic, O. / Quinn, M.T. / Williams, R.L. | ||||||
![]() | ![]() Title: Pb1 Domain-Mediated Heterodimerization in Nadph Oxidase and Signaling Complexes of Atypical Protein Kinase C with Par6 and P62 Authors: Wilson, M.I. / Gill, D.J. / Perisic, O. / Quinn, M.T. / Williams, R.L. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.8 KB | Display | ![]() |
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PDB format | ![]() | 137.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 469.4 KB | Display | ![]() |
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Full document | ![]() | 479 KB | Display | |
Data in XML | ![]() | 29.5 KB | Display | |
Data in CIF | ![]() | 43.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 9940.824 Da / Num. of mol.: 4 / Fragment: PB1 DOMAIN, RESIDUES 352-429 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 12848.079 Da / Num. of mol.: 4 / Fragment: PB1 DOMAIN, RESIDUES 237-339 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.8 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 9 Details: 18% PEG 3350, 17% PEG 400, 4.8% ISOPROPYL ALCOHOL, 0.1 M CAPSO PH 9.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 15, 2002 / Details: BENT MIRROR | ||||||||||||
Radiation | Monochromator: SI(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2→100 Å / Num. obs: 357868 / % possible obs: 97.7 % / Observed criterion σ(I): 1 / Redundancy: 6.1 % / Rmerge(I) obs: 0.155 / Net I/σ(I): 8.6 | ||||||||||||
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.473 / Mean I/σ(I) obs: 1.6 / % possible all: 94 | ||||||||||||
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 59062 / Num. measured all: 357868 / Rmerge(I) obs: 0.155 | ||||||||||||
Reflection shell | *PLUS % possible obs: 94 % / Rmerge(I) obs: 0.473 / Mean I/σ(I) obs: 1.4 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.88 Å2
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Refinement step | Cycle: LAST / Resolution: 2→100 Å
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Refine LS restraints |
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