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- PDB-4za5: Structure of A. niger Fdc1 with the prenylated-flavin cofactor in... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4za5 | ||||||
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Title | Structure of A. niger Fdc1 with the prenylated-flavin cofactor in the iminium and ketimine forms. | ||||||
![]() | Fdc1 | ||||||
![]() | LYASE / (de)carboxylase / prenylated flavin binding / UbiD-type enzyme | ||||||
Function / homology | ![]() styrene metabolic process / aromatic amino acid family catabolic process / phenacrylate decarboxylase / 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity / ferulate metabolic process / cinnamic acid catabolic process / ubiquinone biosynthetic process / manganese ion binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Payne, K.A.P. / Leys, D. | ||||||
![]() | ![]() Title: New cofactor supports alpha , beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Authors: Payne, K.A. / White, M.D. / Fisher, K. / Khara, B. / Bailey, S.S. / Parker, D. / Rattray, N.J. / Trivedi, D.K. / Goodacre, R. / Beveridge, R. / Barran, P. / Rigby, S.E. / Scrutton, N.S. / Hay, S. / Leys, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 244.2 KB | Display | ![]() |
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PDB format | ![]() | 190.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 27.4 KB | Display | |
Data in CIF | ![]() | 41.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4za4C ![]() 4za7C ![]() 4za8C ![]() 4za9C ![]() 4zaaC ![]() 4zabC ![]() 4zacC ![]() 4zadC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 56335.945 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: A2QHE5, 4-hydroxybenzoate decarboxylase |
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-Non-polymers , 5 types, 476 molecules ![](data/chem/img/4LU.gif)
![](data/chem/img/FZZ.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/K.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FZZ.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/K.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-4LU / | ||
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#3: Chemical | ChemComp-FZZ / | ||
#4: Chemical | ChemComp-MN / | ||
#5: Chemical | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.41 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: 0.2 M potassium thiocyanate, Bis-Tris propane 6.5, 20 % w/v PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 13, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 1.1→48.01 Å / Num. obs: 206025 / % possible obs: 99.97 % / Redundancy: 5.5 % / Rmerge(I) obs: 0.032 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 1.1→1.13 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.378 / Mean I/σ(I) obs: 2.1 / % possible all: 99.99 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 10.711 Å2
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Refinement step | Cycle: 1 / Resolution: 1.1→48.01 Å
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Refine LS restraints |
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