+Open data
-Basic information
Entry | Database: PDB / ID: 2l73 | ||||||
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Title | Structure of the NOXO1b PX domain | ||||||
Components | NADPH oxidase organizer 1 | ||||||
Keywords | OXIDOREDUCTASE REGULATOR / Cell membrane / PX domain | ||||||
Function / homology | Function and homology information superoxide-generating NADPH oxidase activator activity / regulation of respiratory burst / NADPH oxidase complex / regulation of hydrogen peroxide metabolic process / WNT5:FZD7-mediated leishmania damping / phosphatidylinositol-3-phosphate binding / superoxide metabolic process / RHO GTPases Activate NADPH Oxidases / extracellular matrix disassembly / phospholipid binding ...superoxide-generating NADPH oxidase activator activity / regulation of respiratory burst / NADPH oxidase complex / regulation of hydrogen peroxide metabolic process / WNT5:FZD7-mediated leishmania damping / phosphatidylinositol-3-phosphate binding / superoxide metabolic process / RHO GTPases Activate NADPH Oxidases / extracellular matrix disassembly / phospholipid binding / enzyme binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Davis, N.Y. / McPhail, L.C. / Horita, D.A. | ||||||
Citation | Journal: To be Published Title: Structure of the NOXO1b PX domain Authors: Davis, N.Y. / McPhail, L.C. / Horita, D.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l73.cif.gz | 633.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l73.ent.gz | 548.1 KB | Display | PDB format |
PDBx/mmJSON format | 2l73.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l7/2l73 ftp://data.pdbj.org/pub/pdb/validation_reports/l7/2l73 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16603.188 Da / Num. of mol.: 1 / Fragment: PX Domain, residues 1-144 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): RIPL / References: UniProt: Q8NFA2 |
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Sequence details | THE DEPOSITED SEQUENCE CORRESPOND |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5mM [U-13C; U-15N; U-2H] protein; 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.5 mM / Component: entity-1 / Isotopic labeling: [U-13C; U-15N; U-2H] |
Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 14 / Conformers submitted total number: 14 / Representative conformer: 1 |