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Open data
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Basic information
Entry | Database: PDB / ID: 1cex | ||||||
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Title | STRUCTURE OF CUTINASE | ||||||
![]() | CUTINASE | ||||||
![]() | SERINE ESTERASE / HYDROLASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Longhi, S. / Czjzek, M. / Lamzin, V. / Nicolas, A. / Cambillau, C. | ||||||
![]() | ![]() Title: Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis. Authors: Longhi, S. / Czjzek, M. / Lamzin, V. / Nicolas, A. / Cambillau, C. #1: ![]() Title: Crystal Structure of Cutinase Covalently Inhibited by a Triglyceride Analogue Authors: Longhi, S. / Mannesse, M. / Verheij, H.M. / De Haas, G.H. / Egmond, M. / Knoops-Mouthuy, E. / Cambillau, C. #2: ![]() 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. #3: ![]() 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. #4: ![]() 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. #5: ![]() 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 | ![]() | 83.5 KB | Display | ![]() |
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PDB format | ![]() | 68.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 395.4 KB | Display | ![]() |
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Full document | ![]() | 399.7 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Data in CIF | ![]() | 10.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 22278.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00590, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases |
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#2: Water | ChemComp-HOH / |
Compound details | THE CATALYTIC SERINE HAS THE EPSILON CONFORMATION WHICH IS TYPICAL OF ALL THE MEMBERS OF THE ...THE CATALYTIC SERINE HAS 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 grow | *PLUS Temperature: 20 ℃ / pH: 7 / Method: vapor diffusion, hanging drop / Details: Abergel, C., (1990) J. Mol. Biol., 215, 215. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.927 Å / Relative weight: 1 |
Reflection | Num. obs: 86474 / % possible obs: 93.3 % / Redundancy: 2.07 % / Rmerge(I) obs: 0.039 |
Reflection | *PLUS Highest resolution: 1 Å / Lowest resolution: 15 Å / Num. measured all: 179064 |
Reflection shell | *PLUS Highest resolution: 1 Å / Lowest resolution: 1.01 Å / % possible obs: 99 % / Rmerge(I) obs: 0.598 / Mean I/σ(I) obs: 2.2 |
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Processing
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Refinement | Resolution: 1→15 Å / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1→15 Å
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Refine LS restraints |
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