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Open data
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Basic information
Entry | Database: PDB / ID: 8cj0 | ||||||
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Title | E. coli NfsB-T41Q/N71S/F124T/M127V mutant bound to nicotinate | ||||||
![]() | Oxygen-insensitive NAD(P)H nitroreductase | ||||||
![]() | OXIDOREDUCTASE / Nitroreductase mutant / complex | ||||||
Function / homology | ![]() oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor / 6,7-dihydropteridine reductase / 2,4,6-trinitrotoluene catabolic process / 6,7-dihydropteridine reductase activity / NAD(P)H dehydrogenase (quinone) activity / Oxidoreductases / FMN binding / protein homodimerization activity / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | White, S.A. / Hyde, E.I. / Day, M.A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and Dynamics of Three Escherichia coli NfsB Nitro-Reductase Mutants Selected for Enhanced Activity with the Cancer Prodrug CB1954. Authors: Day, M.A. / Christofferson, A.J. / Anderson, J.L.R. / Vass, S.O. / Evans, A. / Searle, P.F. / White, S.A. / Hyde, E.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 190.2 KB | Display | ![]() |
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PDB format | ![]() | 149.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 19 KB | Display | |
Data in CIF | ![]() | 26.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8c5eC ![]() 8c5fC ![]() 8c5pC ![]() 8ccvC ![]() 8og3C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23859.045 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: 4 mutations T41Q, N71S, F124T, M127V. / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P38489, Oxidoreductases, 6,7-dihydropteridine reductase #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-EDO / | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.19 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: 12% PEG 4000, 100 mM Na Acetate, 20 mM Nicotinic acid, 15% Ethylene glycol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Jul 28, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→35.06 Å / Num. obs: 31129 / % possible obs: 98.9 % / Redundancy: 9 % / Rsym value: 0.075 / Net I/σ(I): 25.3 |
Reflection shell | Resolution: 1.994→2.046 Å / Redundancy: 8.93 % / Num. unique obs: 2176 / Rsym value: 0.55 / % possible all: 95.4 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.944 Å2
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Refinement step | Cycle: LAST / Resolution: 1.99→35.06 Å
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Refine LS restraints |
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