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- PDB-1id8: NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1id8 | ||||||
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Title | NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED WITH THE VITAMIN B12 NUCLEOTIDE | ||||||
![]() | METHYLASPARTATE MUTASE S CHAIN | ||||||
![]() | ISOMERASE / Coenzyme B12 / Ligand Binding / Nucleotide / Protein NMR spectroscopy / Protein folding | ||||||
Function / homology | ![]() methylaspartate mutase / anaerobic glutamate catabolic process / methylaspartate mutase activity / glutamate catabolic process via L-citramalate / cobalamin binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / restrained simulated annealing, molecular dynamics, energy minimazation | ||||||
![]() | Tollinger, M. / Eichmuller, C. / Konrat, R. / Huhta, M.S. / Marsh, E.N.G. / Krautler, B. | ||||||
![]() | ![]() Title: The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12). Authors: Tollinger, M. / Eichmuller, C. / Konrat, R. / Huhta, M.S. / Marsh, E.N. / Krautler, B. #1: ![]() Title: Adenosylcobalamin-dependent Glutamate Mutase from Clostridium Tetanomorphum. Overexpression in Escherichia coli, Purification, and Characterization of the Recombinant Enzyme Authors: Holloway, D.E. / Marsh, E.N. #2: ![]() Title: How a Protein Prepares for B12 Binding: Structure and Dynamics of the B12-binding Subunit of Glutamate Mutase from Clostridium tetanomorphum Authors: Tollinger, M. / Konrat, R. / Hilbert, B.H. / Marsh, E.N. / Krautler, B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 633.6 KB | Display | ![]() |
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PDB format | ![]() | 516 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 474.9 KB | Display | ![]() |
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Full document | ![]() | 604.7 KB | Display | |
Data in XML | ![]() | 54.5 KB | Display | |
Data in CIF | ![]() | 68 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 14763.856 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FOP / |
#3: Chemical | ChemComp-DBI / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.5mM MutS U-15N; 18.0mM B12-Nucleotide; 10mM potassium phosphate buffer; 90% H2O, 10%D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 10mM potassium phosphate / pH: 6.0 / Pressure: ambient / Temperature: 299 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: restrained simulated annealing, molecular dynamics, energy minimazation Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 30 / Conformers submitted total number: 15 |