+Open data
-Basic information
Entry | Database: PDB / ID: 2adm | |||||||||
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Title | ADENINE-N6-DNA-METHYLTRANSFERASE TAQI | |||||||||
Components | ADENINE-N6-DNA-METHYLTRANSFERASE TAQI | |||||||||
Keywords | METHYLTRANSFERASE / TRANSFERASE / RESTRICTION SYSTEM | |||||||||
Function / homology | Function and homology information site-specific DNA-methyltransferase (adenine-specific) / site-specific DNA-methyltransferase (adenine-specific) activity / DNA restriction-modification system / DNA binding Similarity search - Function | |||||||||
Biological species | Thermus aquaticus (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | |||||||||
Authors | Schluckebier, G. / Saenger, W. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 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: Journal: J.Mol.Biol. / Year: 1995 Title: Universal Catalytic Domain Structure of Adomet-Dependent Methyltransferases Authors: Schluckebier, G. / O'Gara, M. / Saenger, W. / Cheng, X. #2: Journal: Gene / Year: 1995 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. #3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2adm.cif.gz | 167.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2adm.ent.gz | 132.1 KB | Display | PDB format |
PDBx/mmJSON format | 2adm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ad/2adm ftp://data.pdbj.org/pub/pdb/validation_reports/ad/2adm | HTTPS FTP |
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-Related structure data
-Links
-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: (-0.99979, 0.02029, -0.00367), Vector: |
-Components
#1: Protein | Mass: 47931.191 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: S-ADENOSYL-METHIONINE AS LIGAND / Source: (gene. exp.) Thermus aquaticus (bacteria) / Gene: TAQ / Plasmid: PPR594 / Production host: Escherichia coli (E. coli) / Strain (production host): ER1821 References: UniProt: P14385, site-specific DNA-methyltransferase (adenine-specific) #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.08 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 37305 / % possible obs: 94.9 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.066 |
Reflection | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 10 Å / Num. measured all: 220712 |
-Processing
Software |
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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: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_improper_angle_deg / Dev ideal: 1.3 |