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- PDB-1ffb: CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATIO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ffb | ||||||
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Title | CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE | ||||||
![]() | CUTINASE![]() | ||||||
![]() | HYDROLASE (SERINE ESTERASE) | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Cambillau, C. / Martinez, C. / Nicolas, A. | ||||||
![]() | ![]() Title: Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Authors: Nicolas, A. / Egmond, M. / Verrips, C.T. / de Vlieg, J. / Longhi, S. / Cambillau, C. / Martinez, C. #1: ![]() Title: Cutinase, a Lipolytic Enzyme with a Preformed Oxyanion Hole Authors: Martinez, C. / Nicolas, A. / Van Tilbeurgh, H. / Egloff, M.-P. / Cudrey, C. / Verger, R. / Cambillau, C. #2: ![]() Title: Fusarium Solani Cutinase is a Lipolytic Enzyme with a Catalytic Serine Accessible to Solvent Authors: Martinez, C. / De Geus, P. / Lauwereys, M. / Matthyssens, G. / Cambillau, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.7 KB | Display | ![]() |
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PDB format | ![]() | 51.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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
#1: Protein | ![]() Mass: 22366.055 Da / Num. of mol.: 1 / Mutation: N84D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.77 Å3/Da / Density % sol: 30.42 % | ||||||||||||||||||||
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Crystal | *PLUS Density % sol: 32 % | ||||||||||||||||||||
Crystal grow![]() | *PLUS Temperature: 29 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 13, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Num. obs: 15053 / % possible obs: 93.3 % / Observed criterion σ(I): 1 / Redundancy: 3.4 % / Rmerge(I) obs: 0.045 |
Reflection | *PLUS Highest resolution: 1.75 Å / Num. measured all: 50443 / Rmerge(I) obs: 0.045 |
Reflection shell | *PLUS Redundancy: 3.4 % |
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Processing
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Refinement | Resolution: 1.75→6 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 37.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |