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- PDB-4jpx: Crystal structure of phenylalanine hydroxylase S203P mutant from ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4jpx | ||||||
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Title | Crystal structure of phenylalanine hydroxylase S203P mutant from Chromobacterium violaceum | ||||||
![]() | Phenylalanine-4-hydroxylase | ||||||
![]() | OXIDOREDUCTASE / hydroxylase | ||||||
Function / homology | ![]() phenylalanine 4-monooxygenase / phenylalanine 4-monooxygenase activity / L-phenylalanine catabolic process / iron ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ronau, J.A. / Abu-Omar, M.M. / Das, C. | ||||||
![]() | ![]() Title: An additional substrate binding site in a bacterial phenylalanine hydroxylase. Authors: Ronau, J.A. / Paul, L.N. / Fuchs, J.E. / Corn, I.R. / Wagner, K.T. / Liedl, K.R. / Abu-Omar, M.M. / Das, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 134.2 KB | Display | ![]() |
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PDB format | ![]() | 103.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 442.5 KB | Display | ![]() |
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Full document | ![]() | 443.7 KB | Display | |
Data in XML | ![]() | 14 KB | Display | |
Data in CIF | ![]() | 20.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3tcyC ![]() 3tk2C ![]() 3tk4C ![]() 4esmC ![]() 4etlC ![]() 4jpyC ![]() 1ltuS 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: 34049.457 Da / Num. of mol.: 1 / Mutation: S203P Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757 Gene: CV_3180, phhA / Plasmid: pGEX-6P1 / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-PHE / |
#3: Chemical | ChemComp-CO / |
#4: Water | ChemComp-HOH / |
Sequence details | ACCORDING TO UNIPROT SEQUENCE DATABASE, THERE ARE SEQUENCE CONFLICTS AT THESE POSITIONS. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.87 Å3/Da / Density % sol: 34.16 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.1 M Na-HEPES, 0.001 M Magnesium chloride hexahydrate, 0.005 M Nickel (II) chloride hexahydrate, 15% w/v PEG 3,350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Feb 23, 2011 |
Radiation | Monochromator: Si 111 Channel / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→50 Å / Num. obs: 31409 / % possible obs: 92.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 1.6 % / Rmerge(I) obs: 0.04 / Rsym value: 0.04 / Net I/σ(I): 15.5 |
Reflection shell | Resolution: 1.55→1.58 Å / % possible all: 81.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1LTU Resolution: 1.55→22.74 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.949 / SU B: 3.436 / SU ML: 0.057 / Isotropic thermal model: Anisotropic / Cross valid method: THROUGHOUT / ESU R: 0.123 / ESU R Free: 0.091 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.856 Å2
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Refinement step | Cycle: LAST / Resolution: 1.55→22.74 Å
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Refine LS restraints |
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