+Open data
-Basic information
Entry | Database: PDB / ID: 1fug | ||||||
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Title | S-ADENOSYLMETHIONINE SYNTHETASE | ||||||
Components | S-ADENOSYLMETHIONINE SYNTHETASE | ||||||
Keywords | TRANSFERASE / ONE-CARBON METABOLISM / ATP-BINDING / MULTIGENE FAMILY | ||||||
Function / homology | Function and homology information methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine cycle / S-adenosylmethionine biosynthetic process / potassium ion binding / one-carbon metabolic process / magnesium ion binding / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3.2 Å | ||||||
Authors | Fu, Z. / Markham, G.D. / Takusagawa, F. | ||||||
Citation | Journal: J.Biomol.Struct.Dyn. / Year: 1996 Title: Flexible loop in the structure of S-adenosylmethionine synthetase crystallized in the tetragonal modification. Authors: Fu, Z. / Hu, Y. / Markham, G.D. / Takusagawa, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fug.cif.gz | 179.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fug.ent.gz | 145.4 KB | Display | PDB format |
PDBx/mmJSON format | 1fug.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fug_validation.pdf.gz | 379.6 KB | Display | wwPDB validaton report |
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Full document | 1fug_full_validation.pdf.gz | 438.1 KB | Display | |
Data in XML | 1fug_validation.xml.gz | 22.7 KB | Display | |
Data in CIF | 1fug_validation.cif.gz | 32.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fu/1fug ftp://data.pdbj.org/pub/pdb/validation_reports/fu/1fug | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 41867.309 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: TETRAGONAL MODIFICATION / Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0A817, methionine adenosyltransferase |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 5 |
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-Sample preparation
Crystal | Density Matthews: 3.7 Å3/Da / Density % sol: 66 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: unknown | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MACSCIENCE DIP100 / Detector: IMAGE PLATE / Date: Oct 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: 3.2→8 Å / Num. obs: 18581 / % possible obs: 92.4 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.08 |
Reflection shell | Resolution: 3.2→3.3 Å / Redundancy: 2 % / Rmerge(I) obs: 0.11 / Mean I/σ(I) obs: 2.7 / % possible all: 85 |
Reflection | *PLUS Num. all: 20096 / Num. measured all: 52893 |
-Processing
Software |
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Refinement | Resolution: 3.2→8 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 35.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_dihedral_angle_deg / Dev ideal: 25 |