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- PDB-2nqh: High Resolution crystal structure of Escherichia coli endonucleas... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2nqh | ||||||
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Title | High Resolution crystal structure of Escherichia coli endonuclease IV (Endo IV) E261Q mutant | ||||||
![]() | Endonuclease 4 | ||||||
![]() | HYDROLASE / Tim-Barrel / trinuclear zinc center | ||||||
Function / homology | ![]() deoxyribonuclease IV / deoxyribonuclease IV (phage-T4-induced) activity / phosphoric diester hydrolase activity / 3'-5'-DNA exonuclease activity / phosphatase activity / DNA-(apurinic or apyrimidinic site) endonuclease activity / base-excision repair / endonuclease activity / DNA repair / DNA binding ...deoxyribonuclease IV / deoxyribonuclease IV (phage-T4-induced) activity / phosphoric diester hydrolase activity / 3'-5'-DNA exonuclease activity / phosphatase activity / DNA-(apurinic or apyrimidinic site) endonuclease activity / base-excision repair / endonuclease activity / DNA repair / DNA binding / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Garcin-Hosfield, E.D. / Hosfield, D.J. / Tainer, J.A. | ||||||
![]() | ![]() Title: DNA apurinic-apyrimidinic site binding and excision by endonuclease IV. Authors: Garcin, E.D. / Hosfield, D.J. / Desai, S.A. / Haas, B.J. / Bjoras, M. / Cunningham, R.P. / Tainer, J.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 76.1 KB | Display | ![]() |
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PDB format | ![]() | 54.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.4 KB | Display | ![]() |
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Full document | ![]() | 432.9 KB | Display | |
Data in XML | ![]() | 15.9 KB | Display | |
Data in CIF | ![]() | 24.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2nq9C ![]() 2nqjC ![]() 1qtwS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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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: 31517.512 Da / Num. of mol.: 1 / Mutation: E261Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-PO4 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.64 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.9 Details: 20% MPEG-2000, 0.1M HEPES pH 5.9, 0.1mM ZnCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→20 Å / Num. obs: 102718 / % possible obs: 92 % / Rsym value: 0.072 / Net I/σ(I): 19.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1QTW Resolution: 1.1→20 Å / σ(F): 0
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Displacement parameters | Biso mean: 16.723 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→20 Å
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