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Open data
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Basic information
Entry | Database: PDB / ID: 1aqi | ||||||
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Title | STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI | ||||||
![]() | ADENINE-N6-DNA-METHYLTRANSFERASE TAQI | ||||||
![]() | METHYLTRANSFERASE / TRANSFERASE / RESTRICTION SYSTEM | ||||||
Function / homology | ![]() site-specific DNA-methyltransferase (adenine-specific) / site-specific DNA-methyltransferase (adenine-specific) activity / DNA restriction-modification system / methylation / DNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schluckebier, G. / Saenger, W. | ||||||
![]() | ![]() Title: Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI. Authors: Schluckebier, G. / Kozak, M. / Bleimling, N. / Weinhold, E. / Saenger, W. #1: ![]() Title: A Model for DNA Binding and Enzyme Action Derived from Crystallographic Studies of the TaqI N6-Adenine-Methyltransferase Authors: Schluckebier, G. / Labahn, J. / Granzin, J. / Schildkraut, I. / Saenger, W. #2: ![]() Title: Universal Catalytic Domain Structure of Adomet-Dependent Methyltransferases Authors: Schluckebier, G. / O'Gara, M. / Saenger, W. / Cheng, X. #3: ![]() Title: Three-Dimensional Structure of the Adenine-Specific DNA Methyltransferase M.Taq I in Complex with the Cofactor S-Adenosylmethionine Authors: Labahn, J. / Granzin, J. / Schluckebier, G. / Robinson, D.P. / Jack, W.E. / Schildkraut, I. / Saenger, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 165.1 KB | Display | ![]() |
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PDB format | ![]() | 130.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 996.8 KB | Display | ![]() |
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Full document | ![]() | 1015 KB | Display | |
Data in XML | ![]() | 30.3 KB | Display | |
Data in CIF | ![]() | 40.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99993, 0.0114, 0.00167), Vector: |
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Components
#1: Protein | Mass: 47931.191 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P14385, site-specific DNA-methyltransferase (adenine-specific) #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.58 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.3 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 1, 1994 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→10 Å / Num. obs: 30844 / % possible obs: 96 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Rmerge(I) obs: 0.066 |
Reflection | *PLUS Num. measured all: 110392 |
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Processing
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Refinement | Resolution: 2.6→10 Å / σ(F): 1
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Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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