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- PDB-6gi2: Crystal structure of the ferric enterobactin esterase (pfeE) muta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6gi2 | ||||||
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Title | Crystal structure of the ferric enterobactin esterase (pfeE) mutant(S157A) from Pseudomonas aeruginosa in complex with Tris-catechol vector | ||||||
![]() | Ferric enterobactin esterase | ||||||
![]() | HYDROLASE / PfeE / PA2689 | ||||||
Function / homology | ![]() iron(III)-enterobactin esterase / carboxylic ester hydrolase activity / hydrolase activity, acting on ester bonds / periplasmic space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Moynie, L. / Naismith, J.H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: A Key Role for the Periplasmic PfeE Esterase in Iron Acquisition via the Siderophore Enterobactin in Pseudomonas aeruginosa. Authors: Perraud, Q. / Moynie, L. / Gasser, V. / Munier, M. / Godet, J. / Hoegy, F. / Mely, Y. / Mislin, G.L.A. / Naismith, J.H. / Schalk, I.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 125.1 KB | Display | ![]() |
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PDB format | ![]() | 95.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 23.5 KB | Display | |
Data in CIF | ![]() | 33.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6gi0SC ![]() 6gi1C ![]() 6gi5C S: Starting model for refinement 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: VAL / End label comp-ID: VAL / Refine code: _ / Auth seq-ID: 11 - 275 / Label seq-ID: 14 - 278
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 30631.729 Da / Num. of mol.: 2 / Mutation: S157A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 Gene: PA2689 / Production host: ![]() ![]() |
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-Non-polymers , 5 types, 270 molecules ![](data/chem/img/FE.gif)
![](data/chem/img/8SW.gif)
![](data/chem/img/NO3.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/8SW.gif)
![](data/chem/img/NO3.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-EDO / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.57 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion / Details: PEG MME 2000, Sodium acetate, potassium nitrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Apr 27, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 1.48→129.87 Å / Num. obs: 95776 / % possible obs: 100 % / Redundancy: 7.2 % / CC1/2: 0.999 / Rmerge(I) obs: 0.058 / Net I/σ(I): 16.8 |
Reflection shell | Resolution: 1.48→1.51 Å / Redundancy: 7.1 % / Rmerge(I) obs: 0.796 / Mean I/σ(I) obs: 2.2 / Num. unique obs: 4729 / CC1/2: 0.863 / % possible all: 99.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6GI0 Resolution: 1.49→65.98 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.962 / SU B: 1.29 / SU ML: 0.047 / Cross valid method: THROUGHOUT / ESU R: 0.065 / ESU R Free: 0.067 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.077 Å2
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Refinement step | Cycle: 1 / Resolution: 1.49→65.98 Å
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Refine LS restraints |
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