+Open data
-Basic information
Entry | Database: PDB / ID: 3dyo | ||||||
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Title | E. coli (lacZ) beta-galactosidase (H418N) in complex with IPTG | ||||||
Components | Beta-galactosidase | ||||||
Keywords | HYDROLASE / beta-galactosidase / Glycosidase | ||||||
Function / homology | Function and homology information alkali metal ion binding / lactose catabolic process / beta-galactosidase complex / beta-galactosidase / beta-galactosidase activity / carbohydrate binding / magnesium ion binding / identical protein binding Similarity search - Function | ||||||
Biological species | Escherichia coli K12 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Juers, D.H. / Huber, R.E. / Matthews, B.W. | ||||||
Citation | Journal: Protein Sci. / Year: 2009 Title: Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli). Authors: Juers, D.H. / Rob, B. / Dugdale, M.L. / Rahimzadeh, N. / Giang, C. / Lee, M. / Matthews, B.W. / Huber, R.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3dyo.cif.gz | 922.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3dyo.ent.gz | 734.4 KB | Display | PDB format |
PDBx/mmJSON format | 3dyo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dy/3dyo ftp://data.pdbj.org/pub/pdb/validation_reports/dy/3dyo | HTTPS FTP |
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-Related structure data
Related structure data | 3dymC 3dypC 3e1fC 1dp0S 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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-Components
-Protein / Sugars , 2 types, 16 molecules ABCD
#1: Protein | Mass: 116482.234 Da / Num. of mol.: 4 / Mutation: H418N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K12 (bacteria) / Gene: lacZ, b0344, JW0335 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P00722, beta-galactosidase #4: Sugar | ChemComp-IPT / |
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-Non-polymers , 4 types, 3857 molecules
#2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-NA / #5: Chemical | ChemComp-DMS / #6: 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: 2.7 Å3/Da / Density % sol: 54.52 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K |
-Data collection
Diffraction | Mean temperature: 96 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Apr 1, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. all: 452647 / Num. obs: 452647 / % possible obs: 98 % / Observed criterion σ(I): 2 / Redundancy: 3.2 % / Biso Wilson estimate: 21.6 Å2 / Rmerge(I) obs: 0.089 / Rsym value: 0.076 / Net I/σ(I): 6.9 |
Reflection shell | Resolution: 1.8→1.85 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.422 / Mean I/σ(I) obs: 2 / Num. unique all: 32207 / Rsym value: 0.352 / % possible all: 94.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1DP0 Resolution: 1.8→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT
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Displacement parameters | Biso mean: 25.4 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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