+Open data
-Basic information
Entry | Database: PDB / ID: 6guo | |||||||||
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Title | Siderophore hydrolase EstA from Aspergillus nidulans | |||||||||
Components | Putative siderophore-degrading esterase (Eurofung) | |||||||||
Keywords | HYDROLASE / alpha/beta-hydrolase / siderophore / hydrolysis / fungi | |||||||||
Function / homology | : / Esterase-like / Putative esterase / hydrolase activity, acting on ester bonds / Alpha/Beta hydrolase fold / TRIETHYLENE GLYCOL / Siderophore-degrading esterase (Eurofung) Function and homology information | |||||||||
Biological species | Emericella nidulans (mold) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | |||||||||
Authors | Ecker, F. / Haas, H. / Groll, M. / Huber, E.M. | |||||||||
Funding support | Germany, Austria, 2items
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Citation | Journal: Angew. Chem. Int. Ed. Engl. / Year: 2018 Title: Iron Scavenging in Aspergillus Species: Structural and Biochemical Insights into Fungal Siderophore Esterases. Authors: Ecker, F. / Haas, H. / Groll, M. / Huber, E.M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6guo.cif.gz | 517.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6guo.ent.gz | 427.2 KB | Display | PDB format |
PDBx/mmJSON format | 6guo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6guo_validation.pdf.gz | 460.9 KB | Display | wwPDB validaton report |
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Full document | 6guo_full_validation.pdf.gz | 466.4 KB | Display | |
Data in XML | 6guo_validation.xml.gz | 52.9 KB | Display | |
Data in CIF | 6guo_validation.cif.gz | 78 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gu/6guo ftp://data.pdbj.org/pub/pdb/validation_reports/gu/6guo | HTTPS FTP |
-Related structure data
Related structure data | 6gudSC 6gugC 6guiC 6gulC 6gunC 6gupC 6gurC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 33672.832 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (mold) Gene: ANIA_07801 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5AV79 #2: Chemical | ChemComp-PGE / #3: Chemical | ChemComp-CL / #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.5 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Bis-Tris pH 5.5 0.25 M NaCl 20 % PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 18, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→45 Å / Num. obs: 129886 / % possible obs: 99 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 9.6 |
Reflection shell | Resolution: 1.75→1.85 Å / Rmerge(I) obs: 0.556 / Mean I/σ(I) obs: 2.4 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6GUD Resolution: 1.75→15 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.952 / SU B: 5.909 / SU ML: 0.082 / Cross valid method: THROUGHOUT / ESU R: 0.182 / ESU R Free: 0.107 / 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: 27.446 Å2
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Refinement step | Cycle: 1 / Resolution: 1.75→15 Å
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Refine LS restraints |
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