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- PDB-2ix9: Respective role of protein folding and glycosylation in the therm... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ix9 | ||||||
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Title | Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A | ||||||
![]() | FERULOYL ESTERASE A | ||||||
![]() | HYDROLASE / XYLAN DEGRADATION / FERULOYL ESTERASE EC 3.1.1.73 / GLYCOPROTEIN / SERINE ESTERASE | ||||||
Function / homology | ![]() feruloyl esterase / feruloyl esterase activity / pectin catabolic process / cellulose binding / xylan catabolic process / cellulose catabolic process / lipid metabolic process / cell wall macromolecule catabolic process / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sulzenbacher, G. / Benoit, I. | ||||||
![]() | ![]() Title: Respective Importance of Protein Folding and Glycosylation in the Thermal Stability of Recombinant Feruloyl Esterase A. Authors: Benoit, I. / Asther, M. / Sulzenbacher, G. / Record, E. / Marmuse, L. / Parsiegla, G. / Gimbert, I. / Asther, M. / Bignon, C. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127.6 KB | Display | ![]() |
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PDB format | ![]() | 99.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 467.3 KB | Display | ![]() |
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Full document | ![]() | 470.6 KB | Display | |
Data in XML | ![]() | 26.6 KB | Display | |
Data in CIF | ![]() | 39.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hl6SC 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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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.25029, 0.70753, 0.66087), Vector: |
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Components
#1: Protein | Mass: 28372.918 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 22-281 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-EDO / #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50 % |
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Crystal grow | pH: 9.5 Details: 1.8 M AMMONIUM SULPHATE 0.2 M LITHIUM SULPHATE 0.1 M CAPS PH 9.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 12, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→62 Å / Num. obs: 60965 / % possible obs: 98.6 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 14.42 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 1.7→1.79 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 2.3 / % possible all: 90.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2HL6 Resolution: 1.7→74.95 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.945 / SU B: 3.707 / SU ML: 0.062 / Cross valid method: THROUGHOUT / ESU R: 0.091 / ESU R Free: 0.094 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.B FACTORS CORRESPOND TO THE OVERALL B FACTORS EQUAL TO THE RESIDUAL PLUS THE TLS COMPONENT.
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.83 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→74.95 Å
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Refine LS restraints |
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