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- PDB-1yki: The structure of E. coli nitroreductase bound with the antibiotic... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1yki | ||||||
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Title | The structure of E. coli nitroreductase bound with the antibiotic nitrofurazone | ||||||
![]() | Oxygen-insensitive NAD(P)H nitroreductase | ||||||
![]() | OXIDOREDUCTASE / Oxygen-insensitive NAD(P)H nitroreductase | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Race, P.R. / Lovering, A.L. / Green, R.M. / Ossor, A. / White, S.A. / Searle, P.F. / Wrighton, C.J. / Hyde, E.I. | ||||||
![]() | ![]() Title: Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme. Authors: Race, P.R. / Lovering, A.L. / Green, R.M. / Ossor, A. / White, S.A. / Searle, P.F. / Wrighton, C.J. / Hyde, E.I. #1: ![]() Title: The Structure of Escherichia coli Nitroreductase Complexed with Nicotinic Acid: Three Crystal Forms at 1.7 A, 1.8 A and 2.4 A Resolution Authors: Lovering, A.L. / Hyde, E.I. / Searle, P.F. / White, S.A. | ||||||
History |
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Remark 600 | HETEROGEN LIGANDS 1218-1219 ARE ASSOCIATED WITH CHAIN A LIGANDS 2218-2219 ARE ASSOCIATED WITH CHAIN ...HETEROGEN LIGANDS 1218-1219 ARE ASSOCIATED WITH CHAIN A LIGANDS 2218-2219 ARE ASSOCIATED WITH CHAIN B LIGANDS 3218-3219 ARE ASSOCIATED WITH CHAIN C LIGANDS 4218-4220 ARE ASSOCIATED WITH CHAIN D |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 203.7 KB | Display | ![]() |
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PDB format | ![]() | 160.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 43.9 KB | Display | |
Data in CIF | ![]() | 63.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ylrC ![]() 1yluC ![]() 1icuS S: Starting model for refinement C: citing same article ( |
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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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Unit cell |
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 23937.182 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 914 molecules ![](data/chem/img/FMN.gif)
![](data/chem/img/NFZ.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/CIT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NFZ.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/CIT.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-FMN / #3: Chemical | ChemComp-NFZ / #4: Chemical | #5: Chemical | ChemComp-CIT / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.6 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: PEG4000, ethylene glycol, nicotinic acid, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 6, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→40 Å / Num. all: 97110 / Num. obs: 97110 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.5 % / Biso Wilson estimate: 17.1 Å2 / Rsym value: 0.056 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 1.7→1.79 Å / Redundancy: 4.6 % / Mean I/σ(I) obs: 5.8 / Num. unique all: 14083 / Rsym value: 0.118 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1ICU Resolution: 1.7→40 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.957 / SU B: 1.44 / SU ML: 0.049 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.089 / ESU R Free: 0.084 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 11.066 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.744 Å / Total num. of bins used: 20 /
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