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Open data
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Basic information
Entry | Database: PDB / ID: 1cui | ||||||
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Title | CUTINASE, S120A MUTANT | ||||||
![]() | CUTINASE | ||||||
![]() | HYDROLASE (SERINE ESTERASE) / HYDROLASE / SERINE ESTERASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Martinez, C. / Cambillau, C. | ||||||
![]() | ![]() Title: Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Authors: Longhi, S. / Nicolas, A. / Creveld, L. / Egmond, M. / Verrips, C.T. / de Vlieg, J. / Martinez, C. / Cambillau, C. #1: ![]() Title: Contribution of Cutinase Ser 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. #2: ![]() 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. #3: ![]() Title: Engineering Cysteine Mutants to Obtain Crystallographic Phases with a Cutinase from Fusarium Solani Pisi Authors: Martinez, C. / De Geus, P. / Stanssens, P. / Lauwereys, M. / Cambillau, C. #4: ![]() 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 | ![]() | 64.5 KB | Display | ![]() |
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PDB format | ![]() | 51.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 363.4 KB | Display | ![]() |
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Full document | ![]() | 365.6 KB | Display | |
Data in XML | ![]() | 5.5 KB | Display | |
Data in CIF | ![]() | 8.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cuaC ![]() 1cubC ![]() 1cucC ![]() 1cudC ![]() 1cueC ![]() 1cufC ![]() 1cugC ![]() 1cuhC ![]() 1cujC ![]() 1cuuC ![]() 1cuvC ![]() 1cuwC ![]() 1cuxC ![]() 1cuyC ![]() 1cuzC ![]() 1xzaC ![]() 1xzdC ![]() 1xzeC ![]() 1xzfC ![]() 1xzgC ![]() 1xzhC ![]() 1xziC ![]() 1xzjC ![]() 1xzkC ![]() 1xzlC ![]() 1xzmC 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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Unit cell |
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Components
#1: Protein | Mass: 22262.953 Da / Num. of mol.: 1 / Mutation: S120A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Compound details | SER 120: THE "EPSILON" CONFORMATION OF THE CATALYTIC SERINE IS A TYPICAL FEATURE OF THE ALPHA/BETA ...SER 120: THE "EPSILON" CONFORMATI |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37 % | ||||||||||||||||||||
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Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / PH range low: 8 / PH range high: 6 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.5 Å / Num. obs: 23900 / % possible obs: 89 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.061 |
Reflection | *PLUS Highest resolution: 2.7 Å / Num. measured all: 74333 |
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Processing
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Refinement | Resolution: 2.5→8 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 42 Å2 |