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Yorodumi- PDB-1bmt: HOW A PROTEIN BINDS B12: A 3.O ANGSTROM X-RAY STRUCTURE OF THE B1... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bmt | ||||||
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Title | HOW A PROTEIN BINDS B12: A 3.O ANGSTROM X-RAY STRUCTURE OF THE B12-BINDING DOMAINS OF METHIONINE SYNTHASE | ||||||
Components | METHIONINE SYNTHASE | ||||||
Keywords | METHYLTRANSFERASE | ||||||
Function / homology | Function and homology information methionine synthase / methionine synthase activity / homocysteine metabolic process / methionine biosynthetic process / cobalamin binding / tetrahydrofolate metabolic process / tetrahydrofolate interconversion / methylation / zinc ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Drennan, C.L. / Huang, S. / Drummond, J.T. / Matthews, R.G. / Ludwig, M.L. | ||||||
Citation | Journal: Science / Year: 1994 Title: How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase. Authors: Drennan, C.L. / Huang, S. / Drummond, J.T. / Matthews, R.G. / Ludwig, M.L. #1: Journal: Curr.Opin.Struct.Biol. / Year: 1994 Title: Cobalamin-Dependent Methionine Synthase: The Structure of a Methylcobalamin-Binding Fragment and Implications for Other B12-Dependent Enzymes Authors: Drennan, C.L. / Matthews, R.G. / Ludwig, M.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bmt.cif.gz | 111 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bmt.ent.gz | 86 KB | Display | PDB format |
PDBx/mmJSON format | 1bmt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bm/1bmt ftp://data.pdbj.org/pub/pdb/validation_reports/bm/1bmt | HTTPS FTP |
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-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: 27209.154 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P13009, methionine synthase #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE SECONDARY STRUCTURAL ELEMENTS WERE IDENTIFIED BY HYDROGEN BONDING PATTERNS AND THE METHOD OF ...THE SECONDARY STRUCTURAL | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.75 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 3 Å / Num. obs: 10417 / % possible obs: 89 % / Rmerge(I) obs: 0.054 |
Reflection shell | *PLUS Mean I/σ(I) obs: 2 |
-Processing
Software |
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Refinement | Resolution: 3→8 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 3→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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