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Yorodumi- PDB-6cia: Crystal structure of aldo-keto reductase from Klebsiella pneumoni... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6cia | ||||||
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Title | Crystal structure of aldo-keto reductase from Klebsiella pneumoniae in complex with NADPH. | ||||||
Components | Aldo/keto reductase | ||||||
Keywords | OXIDOREDUCTASE / Structural Genomics / PSI-Biology / Center for Structural Genomics of Infectious Diseases / CSGID | ||||||
Function / homology | Function and homology information D-threo-aldose 1-dehydrogenase activity / Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor Similarity search - Function | ||||||
Biological species | Klebsiella pneumoniae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Lipowska, J. / Leung, E.S. / Shabalin, I.G. / Grabowski, M. / Almo, S.C. / Satchell, K.J. / Joachimiak, A. / Lewinski, K. / Minor, W. / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
Funding support | United States, 1items
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Citation | Journal: to be published Title: Crystal structure of of aldo-keto reductase from Klebsiella pneumoniae in complex with NADPH. Authors: Lipowska, J. / Leung, E.S. / Shabalin, I.G. / Grabowski, M. / Almo, S.C. / Satchell, K.J. / Joachimiak, A. / Lewinski, K. / Minor, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6cia.cif.gz | 134.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6cia.ent.gz | 103.6 KB | Display | PDB format |
PDBx/mmJSON format | 6cia.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ci/6cia ftp://data.pdbj.org/pub/pdb/validation_reports/ci/6cia | HTTPS FTP |
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-Related structure data
Related structure data | 4wghS S: Starting model for refinement |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 31768.480 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella pneumoniae (bacteria) Gene: yhdN_4, yhdN, B1727_06910, B4U21_09420, BN49_2327, CAK82_20800, CQB04_18905, CR230_19100, CTI52_15935, CTI54_15930, PMK1_03573, SAMEA3531778_00013 Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL References: UniProt: W9BFN4, UniProt: A6T7Q7*PLUS, Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor |
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#2: Chemical | ChemComp-NDP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.85 % |
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Crystal grow | Temperature: 289.15 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.2 ul of 11 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the Top 96 #90 (0.2 uL 0.1 M Tris: HCl, pH 8.5, 25 % ...Details: 0.2 ul of 11 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the Top 96 #90 (0.2 uL 0.1 M Tris: HCl, pH 8.5, 25 % (w/v) PEG 3350) and 0.1 uL 30%v/v Ethanol (Additive Screen #82) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97856 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 8, 2017 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 13360 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 8.3 % / Biso Wilson estimate: 33.7 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.083 / Rpim(I) all: 0.03 / Rrim(I) all: 0.088 / Rsym value: 0.083 / Net I/av σ(I): 30.9 / Net I/σ(I): 30.9 |
Reflection shell | Resolution: 2.3→2.34 Å / Redundancy: 7 % / Rmerge(I) obs: 1.092 / Mean I/σ(I) obs: 1.9 / Num. unique obs: 649 / CC1/2: 0.838 / Rpim(I) all: 0.438 / Rrim(I) all: 1.178 / Rsym value: 1.092 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4WGH Resolution: 2.3→50 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.924 / SU B: 15.302 / SU ML: 0.201 / Cross valid method: THROUGHOUT / ESU R: 0.49 / ESU R Free: 0.257 / 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: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 43.872 Å2
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Refinement step | Cycle: 1 / Resolution: 2.3→50 Å
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