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Yorodumi- PDB-3kv3: Crystal structure of C151S mutant of Glyceraldehyde-3-phosphate d... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3kv3 | ||||||
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Title | Crystal structure of C151S mutant of Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH 1)from methicillin resistant Staphylococcus aureus MRSA252 complexed with NAD and G3P | ||||||
Components | GAPDHGlyceraldehyde 3-phosphate dehydrogenase | ||||||
Keywords | OXIDOREDUCTASE / glycolysis | ||||||
Function / homology | Function and homology information glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glycolytic process / glucose metabolic process / NAD binding / NADP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Staphylococcus aureus subsp. aureus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.5 Å | ||||||
Authors | Mukherjee, S. / Dutta, D. / Saha, B. / Das, A.K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2010 Title: Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 1 from methicillin-resistant Staphylococcus aureus MRSA252 provides novel insights into substrate binding and catalytic mechanism. Authors: Mukherjee, S. / Dutta, D. / Saha, B. / Das, A.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3kv3.cif.gz | 267.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3kv3.ent.gz | 217.9 KB | Display | PDB format |
PDBx/mmJSON format | 3kv3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kv/3kv3 ftp://data.pdbj.org/pub/pdb/validation_reports/kv/3kv3 | HTTPS FTP |
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-Related structure data
Related structure data | 3hq4C 3k73C 3k9qC 3ksdC 3kszC 3l4sC 3l6oC 3lc1C 3lc2C 3lc7C 3lvfC 3h48 S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 2 / Auth seq-ID: 2 - 334 / Label seq-ID: 2 - 334
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-Components
#1: Protein | Mass: 36304.699 Da / Num. of mol.: 4 / Mutation: C151S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus subsp. aureus (bacteria) Strain: MRSA252 / Gene: gap, gap1, gapA, gapA1, SAR0828 / Plasmid: pQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15 References: UniProt: Q6GIL8, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) #2: Chemical | ChemComp-NAD / #3: Chemical | ChemComp-3PG / #4: Water | ChemComp-HOH / | Nonpolymer details | THE 3PG IS NOT PHOSPHOGLYCERIC ACID STRUCTURALLY. THE LIGAND BOUND IS THE GEM DI-OL FORM OF ...THE 3PG IS NOT PHOSPHOGLY | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.46 % / Mosaicity: 0.944 ° |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.2 Details: 0.1 (M) Tris-HCl, pH 8.2, 26% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jun 22, 2009 / Details: Varimax mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→86.71 Å / Num. obs: 41759 / % possible obs: 98.8 % / Redundancy: 3.73 % / Biso Wilson estimate: 54.2 Å2 / Rmerge(I) obs: 0.084 / Χ2: 1.01 / Net I/σ(I): 9.7 / Scaling rejects: 1179 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3.71 % / Rmerge(I) obs: 0.344 / Mean I/σ(I) obs: 3.2 / Num. measured all: 15373 / Num. unique all: 4116 / Χ2: 1.17 / % possible all: 97.7 |
-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3H48 3h48 Resolution: 2.5→21.35 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.918 / WRfactor Rfree: 0.219 / WRfactor Rwork: 0.174 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.838 / SU B: 22.248 / SU ML: 0.231 / SU R Cruickshank DPI: 0.256 / SU Rfree: 0.315 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.314 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 88.08 Å2 / Biso mean: 39.086 Å2 / Biso min: 5.4 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→21.35 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.5→2.565 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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