[English] 日本語
Yorodumi- PDB-3rcb: Crystal structure of the K102E mutant of KijD10, a 3-ketoreductas... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3rcb | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the K102E mutant of KijD10, a 3-ketoreductase from Actinomadura kijaniata in complex with TDP-benzene and NADP | ||||||
Components | Sugar 3-ketoreductase | ||||||
Keywords | SUGAR BINDING PROTEIN / sugar biosynthesis / ketoreductase / TDP binding / NADP binding | ||||||
Function / homology | Function and homology information dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase / antibiotic biosynthetic process / oxidoreductase activity / nucleotide binding Similarity search - Function | ||||||
Biological species | Actinomadura kijaniata (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.49 Å | ||||||
Authors | Holden, H.M. / Kubiak, R.L. | ||||||
Citation | Journal: Biochemistry / Year: 2011 Title: Combined Structural and Functional Investigation of a C-3''-Ketoreductase Involved in the Biosynthesis of dTDP-l-Digitoxose. Authors: Kubiak, R.L. / Holden, H.M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 3rcb.cif.gz | 85.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb3rcb.ent.gz | 61.7 KB | Display | PDB format |
PDBx/mmJSON format | 3rcb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rc/3rcb ftp://data.pdbj.org/pub/pdb/validation_reports/rc/3rcb | HTTPS FTP |
---|
-Related structure data
Related structure data | 3rbvSC 3rc1C 3rc2C 3rc7C 3rc9C C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 39262.230 Da / Num. of mol.: 1 / Mutation: K102E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Actinomadura kijaniata (bacteria) / Gene: KijD10 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2 / References: UniProt: B3TMR8 |
---|
-Non-polymers , 6 types, 169 molecules
#2: Chemical | ChemComp-NAP / | ||
---|---|---|---|
#3: Chemical | ChemComp-CL / | ||
#4: Chemical | ChemComp-NA / | ||
#5: Chemical | ChemComp-PO4 / | ||
#6: Chemical | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.46 Å3/Da / Density % sol: 64.47 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 1.2 M sodium/potassium phosphate, 100 mM HEPPS, 5 mM TDP-benzene, 5 mM NADP, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Jan 26, 2011 / Details: montel mirrors |
Radiation | Monochromator: Nickel filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.49→84.27 Å / Num. all: 18970 / Num. obs: 18970 / % possible obs: 96.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.096 / Rsym value: 0.096 / Net I/σ(I): 10.6 |
Reflection shell | Resolution: 2.49→2.58 Å / Redundancy: 10.6 % / Rmerge(I) obs: 0.238 / Mean I/σ(I) obs: 3.2 / Num. unique all: 1756 / Rsym value: 0.238 / % possible all: 86.9 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: model generated using binary complex, PDB entry 3RBV Resolution: 2.49→65 Å / Cor.coef. Fo:Fc: 0.924 / Cor.coef. Fo:Fc free: 0.867 / SU B: 6.844 / SU ML: 0.155 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.251 / Stereochemistry target values: MAXIMUM LIKELIHOOD
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 mean: 17.118 Å2
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.49→65 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.49→2.553 Å / Total num. of bins used: 20
|