+Open data
-Basic information
Entry | Database: PDB / ID: 3muz | ||||||
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Title | E.Coli (lacZ) beta-galactosidase (R599A) in complex with IPTG | ||||||
Components | Beta-galactosidase | ||||||
Keywords | HYDROLASE / Arg-599-Ala / BETA-GALACTOSIDASE / HYDROLASE TIM BARREL(ALPHA/BETA BARREL) / JELLY-ROLL BARREL / IMMUNOGLOBULIN BETA SUPERSANDWHICH / GLYCOSIDASE | ||||||
Function / homology | Function and homology information alkali metal ion binding / organic substance catabolic process / lactose catabolic process / beta-galactosidase complex / beta-galactosidase / beta-galactosidase activity / carbohydrate binding / carbohydrate metabolic process / magnesium ion binding / identical protein binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Dugdale, M.L. / Vance, M.L. / Driedger, M.R. / Nibber, A. / Tran, A. / Huber, R.E. | ||||||
Citation | Journal: Biochem.Cell Biol. / Year: 2010 Title: Importance of Arg-599 of b-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop Authors: Dugdale, M.L. / Vance, M.L. / Wheatley, R.W. / Driedger, M.R. / Nibber, A. / Tran, A. / 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 | 3muz.cif.gz | 938.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3muz.ent.gz | 746.3 KB | Display | PDB format |
PDBx/mmJSON format | 3muz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/3muz ftp://data.pdbj.org/pub/pdb/validation_reports/mu/3muz | HTTPS FTP |
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-Related structure data
Related structure data | 3mv0C 3mv1C 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, 12 molecules 1234
#1: Protein | Mass: 119657.633 Da / Num. of mol.: 4 / Mutation: R599A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: lac z / Plasmid: pBAD/HIS/LacZ / Production host: Escherichia coli (E. coli) / Strain (production host): LMG 194 References: UniProt: B8LFD6, UniProt: P00722*PLUS, beta-galactosidase #2: Sugar | ChemComp-IPT / |
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-Non-polymers , 4 types, 4288 molecules
#3: Chemical | ChemComp-MG / #4: 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: 2.64 Å3/Da / Density % sol: 53.48 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: PEG8000, NaCl, MgCl2, DTT, Bis-Tris, pH6.5, HANGING DROP AT 288K, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Aug 22, 2008 / Details: KOHZU: Double Crystal SI(111) |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.11587 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→12.42 Å / Num. obs: 56045 / % possible obs: 98.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.05 % / Biso Wilson estimate: 13.9 Å2 / Limit h max: 79 / Limit h min: 0 / Limit k max: 85 / Limit k min: 0 / Limit l max: 107 / Limit l min: 0 / Observed criterion F max: 6171475.65 / Observed criterion F min: 24.2 / Rmerge(I) obs: 0.116 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.609 / Mean I/σ(I) obs: 2.7 / Num. unique all: 56045 / % possible all: 97.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1DP0 Resolution: 1.9→12.42 Å / Rfactor Rfree error: 0.003 / Occupancy max: 1 / Occupancy min: 0.88 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: CNS bulk solvent model used / Bsol: 68.2735 Å2 / ksol: 0.4 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 109.05 Å2 / Biso mean: 22.74 Å2 / Biso min: 5.69 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→12.42 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION
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