+Open data
-Basic information
Entry | Database: PDB / ID: 1hn1 | ||||||
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Title | E. COLI (LAC Z) BETA-GALACTOSIDASE (ORTHORHOMBIC) | ||||||
Components | BETA-GALACTOSIDASE | ||||||
Keywords | HYDROLASE / ALPHA/BETA BARREL / JELLY ROLL BARREL / FIBRONECTIN / BETA SUPERSANDWICH | ||||||
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 (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Juers, D.H. / Matthews, B.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions. Authors: Juers, D.H. / Matthews, B.W. #1: Journal: Protein Sci. / Year: 2000 Title: High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation Authors: JUERS, D.H. / JACOBSON, R.H. / WIGLEY, D. / ZHANG, X.J. / HUBER, R.E. / TRONRUD, D.E. / MATTHEWS, B.W. #2: Journal: Protein Sci. / Year: 1999 Title: Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases Authors: JUERS, D.H. / HUBER, R.E. / MATTHEWS, B.W. #3: Journal: Nature / Year: 1994 Title: Three-dimensional structure of beta-galactosidase from E. coli. Authors: JACOBSON, R.H. / ZHANG, X.J. / DUBOSE, R.F. / MATTHEWS, B.W. #4: Journal: J.Mol.Biol. / Year: 1992 Title: Crystallization of beta-galactosidase from Escherichia coli. Authors: JACOBSON, R.H. / MATTHEWS, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hn1.cif.gz | 822.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hn1.ent.gz | 664.4 KB | Display | PDB format |
PDBx/mmJSON format | 1hn1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hn/1hn1 ftp://data.pdbj.org/pub/pdb/validation_reports/hn/1hn1 | HTTPS FTP |
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-Related structure data
Related structure data | 1dp0S 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
#1: Protein | Mass: 116506.266 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: LAC Z / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 References: UniProt: P00722, 4-hydroxybenzoyl-CoA thioesterase #2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-NA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.89 Å3/Da / Density % sol: 57.47 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 10% PEG 8000, 100 mM BIS TRIS, 200 mM MGCL(2), 100 mM NACL, 10 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusionDetails: Juers, D.H., (2000) Protein Sci., 9, 1685., used seeding | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Aug 1, 1999 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 3→23 Å / Num. all: 103758 / Num. obs: 103758 / % possible obs: 95.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 7.2 |
Reflection shell | Highest resolution: 3 Å / Rmerge(I) obs: 0.292 / Mean I/σ(I) obs: 2.3 / % possible all: 98.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1DP0 Resolution: 3→15 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT
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Solvent computation | Solvent model: BABINET'S PRINCIPLE / Bsol: 200 Å2 / ksol: 0.75 e/Å3 | |||||||||||||||||||||||||||
Displacement parameters | Biso mean: -0.3 Å2
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Refinement step | Cycle: LAST / Resolution: 3→15 Å
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Refine LS restraints |
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