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- PDB-3wfb: Reduced cytochrome c-dependent nitric oxide reductase (cNOR) from... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3wfb | ||||||
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Title | Reduced cytochrome c-dependent nitric oxide reductase (cNOR) from Pseudomonas aeruginosa in complex with antibody fragment | ||||||
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![]() | IMMUNE SYSTEM/OXIDOREDUCTASE / metal-binding / membrane protein / IMMUNE SYSTEM-OXIDOREDUCTASE complex | ||||||
Function / homology | ![]() nitric oxide reductase (cytochrome c) / nitric oxide reductase activity / denitrification pathway / cytochrome-c oxidase activity / electron transport coupled proton transport / : / aerobic respiration / respiratory electron transport chain / electron transfer activity / heme binding ...nitric oxide reductase (cytochrome c) / nitric oxide reductase activity / denitrification pathway / cytochrome-c oxidase activity / electron transport coupled proton transport / : / aerobic respiration / respiratory electron transport chain / electron transfer activity / heme binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sato, N. / Ishii, S. / Hino, T. / Sugimoto, H. / Fukumori, Y. / Shiro, Y. / Tosha, T. | ||||||
![]() | ![]() Title: Structures of reduced and ligand-bound nitric oxide reductase provide insights into functional differences in respiratory enzymes. Authors: Sato, N. / Ishii, S. / Sugimoto, H. / Hino, T. / Fukumori, Y. / Sako, Y. / Shiro, Y. / Tosha, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 427.9 KB | Display | ![]() |
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PDB format | ![]() | 352.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3wfcC ![]() 3wfdC ![]() 3wfeC ![]() 3o0rS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Nitric oxide reductase subunit ... , 2 types, 2 molecules BC
#3: Protein | Mass: 52215.871 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: Q59647, nitric oxide reductase (cytochrome c) |
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#4: Protein | Mass: 16374.622 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Antibody , 2 types, 2 molecules LH
#1: Antibody | Mass: 23735.326 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Antibody | Mass: 24089.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 6 types, 140 molecules ![](data/chem/img/HEM.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Chemical | ChemComp-FE / | #7: Chemical | ChemComp-CL / | #8: Chemical | ChemComp-CA / | #9: Chemical | ChemComp-HEC / | #10: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.17 Å3/Da / Density % sol: 70.53 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion / pH: 6 Details: 100 mM sodium citrate, pH 6.0, vapor diffusion, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Feb 10, 2011 / Details: mirrors |
Diffraction measurement | Details: 0.50 degrees, 1.7 sec, detector distance 250.00 mm / Method: \w scans |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Av R equivalents: 0.077 / Number: 216044 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 54416 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4 % / Rmerge(I) obs: 0.077 / Rsym value: 0.077 / Net I/σ(I): 15.966 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.823 / Mean I/σ(I) obs: 1.8 / Rsym value: 0.823 / % possible all: 99.5 |
Cell measurement | Reflection used: 216044 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3O0R Resolution: 2.7→41.07 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.904 / Occupancy max: 1 / Occupancy min: 0.72 / SU B: 25.378 / SU ML: 0.23 / Cross valid method: THROUGHOUT / ESU R: 0.379 / ESU R Free: 0.277 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 80.461 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→41.07 Å
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