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- PDB-1ccw: STRUCTURE OF THE COENZYME B12 DEPENDENT ENZYME GLUTAMATE MUTASE F... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ccw | |||||||||
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Title | STRUCTURE OF THE COENZYME B12 DEPENDENT ENZYME GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM | |||||||||
![]() | (PROTEIN (GLUTAMATE MUTASE)) x 2 | |||||||||
![]() | ISOMERASE / GLUTAMATE MUTASE / COENZYME B12 / RADICAL REACTION / TIM-BARREL / ROSSMAN-FOLD | |||||||||
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 | ![]() ![]() ![]() | |||||||||
![]() | Reitzer, R. / Gruber, K. / Kratky, C. | |||||||||
![]() | ![]() Title: Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights Authors: Reitzer, R. / Gruber, K. / Jogl, G. / Wagner, U.G. / Bothe, H. / Buckel, W. / Kratky, C. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1998 Title: Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium. Authors: Reitzer, R. / Krasser, M. / Jogl, G. / Buckel, W. / Bothe, H. / Kratky, C. #2: Journal: Eur.J.Biochem. / Year: 1994 Title: Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. Authors: Zelder, O. / Beatrix, B. / Leutbecher, U. / Buckel, 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 | ![]() | 302.2 KB | Display | ![]() |
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PDB format | ![]() | 237.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 553.3 KB | Display | ![]() |
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Full document | ![]() | 575 KB | Display | |
Data in XML | ![]() | 27.6 KB | Display | |
Data in CIF | ![]() | 51.1 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.980228, -0.006307, 0.197767), Vector: |
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Components
#1: Protein | Mass: 14830.046 Da / Num. of mol.: 2 / Fragment: B12-Binding Subunit Source method: isolated from a genetically manipulated source Details: CHAINS A, C, B, D FORM HETEROTETRAMER WHICH IS THE BIOLOGICAL UNIT Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 53623.172 Da / Num. of mol.: 2 / Fragment: E chain Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH CO-CYANOCOBALAMIN / Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.9 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 4.6 / Details: pH 4.6, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 105 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9058 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. all: 190420 / Num. obs: 190420 / % possible obs: 94.1 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rmerge(I) obs: 0.031 / Rsym value: 0.065 / Net I/σ(I): 5.4 |
Reflection shell | Resolution: 1.6→1.69 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.175 / Mean I/σ(I) obs: 2.7 / Rsym value: 0.173 / % possible all: 94.1 |
Reflection | *PLUS Num. measured all: 441525 / Rmerge(I) obs: 0.065 |
Reflection shell | *PLUS % possible obs: 94.1 % / Rmerge(I) obs: 0.173 |
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Processing
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Refinement | Method to determine structure: ![]() Details: ANISOTROPIC SCALING APPLIED BY THE METHOD OF PARKIN, MOEZZI & HOPE, J. APPL. CRYST. 28 (1995) 53-56
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Solvent computation | Solvent model: MOEWS & KRETSINGER | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 7 / Occupancy sum hydrogen: 9641.9 / Occupancy sum non hydrogen: 11680 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→30 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.136 / Rfactor obs: 0.123 / Rfactor Rfree: 0.171 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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