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Yorodumi- PDB-3k7p: Structure of mutant of ribose 5-phosphate isomerase type B from T... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3k7p | ||||||
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Title | Structure of mutant of ribose 5-phosphate isomerase type B from Trypanosoma cruzi. | ||||||
Components | Ribose 5-phosphate isomerase | ||||||
Keywords | ISOMERASE / pentose phosphate pathway / Type B ribose 5-phosphate isomerase (RpiB) / R5P / phosphate | ||||||
Function / homology | Function and homology information isomerase activity / carbohydrate metabolic process / identical protein binding Similarity search - Function | ||||||
Biological species | Trypanosoma cruzi (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.4 Å | ||||||
Authors | Naworyta, A. / Mowbray, S.L. / Stern, A.L. | ||||||
Citation | Journal: Febs J. / Year: 2011 Title: Structures of type B ribose 5-phosphate isomerase from Trypanosoma cruzi shed light on the determinants of sugar specificity in the structural family. Authors: Stern, A.L. / Naworyta, A. / Cazzulo, J.J. / Mowbray, S.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3k7p.cif.gz | 75.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3k7p.ent.gz | 56 KB | Display | PDB format |
PDBx/mmJSON format | 3k7p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k7/3k7p ftp://data.pdbj.org/pub/pdb/validation_reports/k7/3k7p | HTTPS FTP |
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-Related structure data
Related structure data | 3k7oC 3k7sC 3k8cC 3m1pC 1nn4S C: citing same article (ref.) S: Starting model for refinement |
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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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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 19527.260 Da / Num. of mol.: 2 / Mutation: C69A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma cruzi (eukaryote) / Strain: strain CL Brener / Gene: 110984573 / Plasmid: pET-28a(+) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS References: UniProt: A1BTJ7, UniProt: Q4CQE2*PLUS, ribose-5-phosphate isomerase #2: Chemical | #3: Water | ChemComp-HOH / | |
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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: 2.6 Å3/Da / Density % sol: 52.72 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.2 Details: 0.8 M Na/K phosphate, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 27, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→30 Å / Num. obs: 79637 / % possible obs: 98.2 % / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Rmerge(I) obs: 0.097 / Rsym value: 0.097 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 1.4→1.48 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.335 / Mean I/σ(I) obs: 3.1 / Num. unique all: 11693 / Rsym value: 0.335 / % possible all: 100 |
-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 1NN4 Resolution: 1.4→30 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.939 / WRfactor Rfree: 0.251 / WRfactor Rwork: 0.242 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.856 / SU B: 1.004 / SU ML: 0.041 / SU R Cruickshank DPI: 0.064 / SU Rfree: 0.062 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.064 / ESU R Free: 0.062 / 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: 49.84 Å2 / Biso mean: 16.949 Å2 / Biso min: 8.48 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.4→1.436 Å / Total num. of bins used: 20
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