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- PDB-4ixw: Halohydrin dehalogenase (HheC) bound to ethyl (2S)-oxiran-2-ylacetate -
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Open data
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Basic information
Entry | Database: PDB / ID: 4ixw | ||||||
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Title | Halohydrin dehalogenase (HheC) bound to ethyl (2S)-oxiran-2-ylacetate | ||||||
![]() | Halohydrin dehalogenase | ||||||
![]() | LYASE / thermostability / synergistic mutations / coupled mutations / proline-induced / backbone changes / enantioselectivity changes / directed evolution / protein engineering / short-chain dehydrogenase/reductase enzyme superfamily / Cyanolysis / dehalogenase / Atorvastatin synthesis | ||||||
Function / homology | Enoyl-(Acyl carrier protein) reductase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / ethyl (2S)-oxiran-2-ylacetate / Halohydrin dehalogenase![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Floor, R.J. / Schallmey, M. / Hauer, B. / Breuer, M. / Jekel, P.A. / Wijma, H.J. / Dijkstra, B.W. / Janssen, D.B. | ||||||
![]() | ![]() Title: Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase. Authors: Schallmey, M. / Floor, R.J. / Hauer, B. / Breuer, M. / Jekel, P.A. / Wijma, H.J. / Dijkstra, B.W. / Janssen, D.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.3 KB | Display | ![]() |
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PDB format | ![]() | 84.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 459.9 KB | Display | ![]() |
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Full document | ![]() | 466.2 KB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 27.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4ixtC ![]() 4iy1C ![]() 1pwzS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27841.406 Da / Num. of mol.: 2 / Fragment: Halohydrin dehalogenase HheC Mutation: Q37H, K38Q, K52I, A60V, Y70L, Q72H, V75I, F82A, A83P, P84V, F86W, Q87R, G99D, A100M, R107K, V112A, K121R, T134A, P135S, T146A, C153S, T154A, Y166H, G174A, Y177G, L178V, H179D, E181G, F186Y, ...Mutation: Q37H, K38Q, K52I, A60V, Y70L, Q72H, V75I, F82A, A83P, P84V, F86W, Q87R, G99D, A100M, R107K, V112A, K121R, T134A, P135S, T146A, C153S, T154A, Y166H, G174A, Y177G, L178V, H179D, E181G, F186Y, T189S, N195S, V201W, K203R, V205Y, A222T, M245V, I246V Source method: isolated from a genetically manipulated source Details: This enzyme is a result of a directed evolution study. It contains 37 mutations, compared to its parent Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.42 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 12.5% (w/v) PEG 8000,0.2 M Magnesium Chloride, 0.1 M Tris-Cl pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 20, 2010 |
Radiation | Monochromator: Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9395 Å / Relative weight: 1 |
Reflection | Resolution: 2.47→63.51 Å / Num. obs: 24644 / % possible obs: 98.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 4.9 / Redundancy: 5.2 % / Rmerge(I) obs: 0.07 / Rsym value: 0.07 / Net I/σ(I): 14 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB code 1PWZ Resolution: 2.47→63.51 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.893 / SU B: 8.866 / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.385 / ESU R Free: 0.284 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.727 Å2
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Refinement step | Cycle: LAST / Resolution: 2.47→63.51 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.47→2.538 Å / Total num. of bins used: 20
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