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- PDB-1n7h: Crystal Structure of GDP-mannose 4,6-dehydratase ternary complex ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1n7h | ||||||
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Title | Crystal Structure of GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP | ||||||
![]() | GDP-D-mannose-4,6-dehydratase | ||||||
![]() | LYASE / Rossmann fold / SDR / short-chain dehydrogenase/reductase | ||||||
Function / homology | ![]() GDP-mannose 4,6-dehydratase / GDP-mannose 4,6-dehydratase activity / GDP-mannose metabolic process / unidimensional cell growth / 'de novo' GDP-L-fucose biosynthetic process / GTP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mulichak, A.M. / Bonin, C.P. / Reiter, W.-D. / Garavito, R.M. | ||||||
![]() | ![]() Title: The structure of the MUR1 GDP-mannose 4,6-dehydratase from A. thaliana: Implications for ligand binding and specificity. Authors: Mulichak, A.M. / Bonin, C.P. / Reiter, W.-D. / Garavito, R.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 156.8 KB | Display | ![]() |
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PDB format | ![]() | 121.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Components on special symmetry positions |
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Details | The biological assembly is a tetramer generated from the dimer in the asymmetric unit by the transformation: -x+1, y, -z+1/2 |
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Components
#1: Protein | Mass: 43084.305 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.42 % | |||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.4 Details: ammonium sulfate, PEG 400, Imidazole buffer, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||
Crystal grow | *PLUS | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: BRANDEIS - B4 / Detector: CCD / Date: Oct 10, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→10 Å / Num. all: 70812 / Num. obs: 70104 / % possible obs: 95 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Rsym value: 0.063 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 4 % / Num. unique all: 6532 / Rsym value: 0.077 / % possible all: 88 |
Reflection | *PLUS Lowest resolution: 10 Å / Num. obs: 70780 / % possible obs: 95 % / Rmerge(I) obs: 0.062 |
Reflection shell | *PLUS % possible obs: 88 % / Rmerge(I) obs: 0.077 |
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Processing
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Refinement | Method to determine structure: ![]() Details: Partial or no side chain atoms were refined for residues listed in REMARK 470.
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Refine analyze | Luzzati coordinate error obs: 0.18 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.86 Å
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Refinement | *PLUS Lowest resolution: 10 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.201 / Rfactor Rwork: 0.18 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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