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- PDB-1xzb: FUSARIUM SOLANI CUTINASE MUTANT WITH SER 129 REPLACED BY CYS COMP... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xzb | ||||||
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Title | FUSARIUM SOLANI CUTINASE MUTANT WITH SER 129 REPLACED BY CYS COMPLEX WITH MERCURY ACETATE | ||||||
![]() | CUTINASE | ||||||
![]() | HYDROLASE (SERINE ESTERASE) / HYDROLASE / SERINE ESTERASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Longhi, S. / Cambillau, C. | ||||||
![]() | ![]() Title: Core Accessibility of Fusarium Solani Pisi Cutinase Explored by Means of Hg Derivatives of the S129C Mutant Authors: Longhi, S. / Martinez, C. / Nicolas, A. / Cambillau, C. #1: ![]() Title: Dynamics of Fusarium Solani Cutinase Investigated Through Structural Comparison Among Different Crystal Forms of 34 Variants Authors: Longhi, S. / Nicolas, A. / Egmond, M. / Verrips, C.T. / Devlieg, J. / Creveld, L. / Martinez, C. / Cambillau, C. #2: ![]() 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. #3: ![]() 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. #4: ![]() 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. #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 | ![]() | 66.6 KB | Display | ![]() |
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PDB format | ![]() | 52.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 629.4 KB | Display | ![]() |
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Full document | ![]() | 633.4 KB | Display | |
Data in XML | ![]() | 12.4 KB | Display | |
Data in CIF | ![]() | 17.7 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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Unit cell |
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Components
#1: Protein | Mass: 22367.082 Da / Num. of mol.: 1 / Mutation: S129C Source method: isolated from a genetically manipulated source Details: COMPLEX WITH MERCURY ACETATE (MAC) / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00590, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE "EPSILON" CONFORMATION OF THE CATALYTIC SERINE IS A TYPICAL FEATURE OF THE ALPHA/BETA HYDROLASE ...THE "EPSILON" CONFORMATI | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.95 Å3/Da / Density % sol: 37 % |
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MAR scanner 180 mm plate / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 15907 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Resolution: 1.75→6 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.75→6 Å
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Refine LS restraints |
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