+Open data
-Basic information
Entry | Database: PDB / ID: 6af6 | ||||||
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Title | PigA with FAD and proline | ||||||
Components | L-prolyl-[peptidyl-carrier protein] dehydrogenase | ||||||
Keywords | BIOSYNTHETIC PROTEIN / red pigment / pyrrole / acyl-CoA oxidase / FAD / tetramer | ||||||
Function / homology | Function and homology information L-prolyl-[peptidyl-carrier protein] dehydrogenase / oxidoreductase activity, acting on the CH-CH group of donors / antibiotic biosynthetic process / flavin adenine dinucleotide binding Similarity search - Function | ||||||
Biological species | Serratia sp. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.62 Å | ||||||
Authors | Lee, C.-C. / Ko, T.-P. / Wang, A.H.J. | ||||||
Funding support | Taiwan, 1items
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Citation | Journal: Chembiochem / Year: 2019 Title: Crystal Structure of PigA: A Prolyl Thioester-Oxidizing Enzyme in Prodigiosin Biosynthesis. Authors: Lee, C.-C. / Ko, T.-P. / Chen, C.T. / Chan, Y.T. / Lo, S.Y. / Chang, J.Y. / Chen, Y.W. / Chung, T.F. / Hsieh, H.J. / Hsiao, C.D. / Wang, A.H.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6af6.cif.gz | 110.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6af6.ent.gz | 80.4 KB | Display | PDB format |
PDBx/mmJSON format | 6af6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/af/6af6 ftp://data.pdbj.org/pub/pdb/validation_reports/af/6af6 | HTTPS FTP |
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-Related structure data
Related structure data | 5zw0C 5zw2C 5zw7C 5zw8SC C: citing same article (ref.) 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 on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 43892.082 Da / Num. of mol.: 1 / Mutation: E244A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Serratia sp. (strain ATCC 39006) (bacteria) Strain: ATCC 39006 / Gene: pigA / Production host: Escherichia coli (E. coli) References: UniProt: Q5W271, L-prolyl-[peptidyl-carrier protein] dehydrogenase |
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-Non-polymers , 6 types, 511 molecules
#2: Chemical | ChemComp-FAD / | ||||||||
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#3: Chemical | #4: Chemical | ChemComp-CL / | #5: Chemical | #6: Chemical | ChemComp-GLY / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.07 Å3/Da / Density % sol: 59.88 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 4 Details: 5mM L-prolylglycine, 1.6M (NH4)2SO4, 2% PEG 400, 0.1M citric acid |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: TPS 05A / Wavelength: 1 Å |
Detector | Type: RAYONIX MX300-HS / Detector: CCD / Date: Jul 26, 2018 |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.62→20 Å / Num. obs: 68585 / % possible obs: 99.8 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 30.2 |
Reflection shell | Resolution: 1.62→1.68 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.537 / Mean I/σ(I) obs: 3.2 / Num. unique obs: 6722 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5ZW8 Resolution: 1.62→19.516 Å / SU ML: 0.12 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 17.65
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.62→19.516 Å
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Refine LS restraints |
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LS refinement shell |
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