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- PDB-6cfu: Structure of Human alpha-Phosphomannomutase 1 containing mutation... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6cfu | ||||||
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Title | Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K | ||||||
![]() | Phosphomannomutase 1 | ||||||
![]() | ISOMERASE / phosphatase / haloalkanoate dehalogenase superfamily / mutase | ||||||
Function / homology | ![]() Synthesis of GDP-mannose / phosphomannomutase / phosphomannomutase activity / GDP-mannose biosynthetic process / mannose metabolic process / protein N-linked glycosylation / cellular response to leukemia inhibitory factor / neuronal cell body / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ji, T. / Dunaway-Mariano, D. / Allen, K.N. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions. Authors: Ji, T. / Zhang, C. / Zheng, L. / Dunaway-Mariano, D. / Allen, K.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 67.7 KB | Display | ![]() |
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PDB format | ![]() | 48 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.6 KB | Display | ![]() |
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Full document | ![]() | 430.1 KB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 16.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6cfrC ![]() 6cfsC ![]() 6cftC ![]() 6cfvC ![]() 2fucS S: Starting model for refinement C: citing same article ( |
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Similar 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
#1: Protein | Mass: 29730.783 Da / Num. of mol.: 1 / Mutation: R180K, R183K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.56 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop Details: 20% polyethylene glycol 3350, 0.15 M DL-malate, pH 7.0, 50 mM MgCl2, and 8 mM beta-mercaptoethanol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 21, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 2.24→49.28 Å / Num. obs: 13960 / % possible obs: 98.41 % / Redundancy: 2 % / Net I/σ(I): 9.62 |
Reflection shell | Resolution: 2.24→2.32 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2FUC Resolution: 2.244→49.28 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 26.72
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.244→49.28 Å
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Refine LS restraints |
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LS refinement shell |
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