+
Open data
-
Basic information
Entry | Database: PDB / ID: 1cuh | ||||||
---|---|---|---|---|---|---|---|
Title | CUTINASE, R196E MUTANT | ||||||
![]() | CUTINASE | ||||||
![]() | HYDROLASE (SERINE ESTERASE) / HYDROLASE / SERINE ESTERASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Longhi, S. / 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 63.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 51 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 370.9 KB | Display | |
Data in XML | ![]() | 5.7 KB | Display | |
Data in CIF | ![]() | 9.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cuaC ![]() 1cubC ![]() 1cucC ![]() 1cudC ![]() 1cueC ![]() 1cufC ![]() 1cugC ![]() 1cuiC ![]() 1cujC ![]() 1cuuC ![]() 1cuvC ![]() 1cuwC ![]() 1cuxC ![]() 1cuyC ![]() 1cuzC ![]() 1xzaC ![]() 1xzdC ![]() 1xzeC ![]() 1xzfC ![]() 1xzgC ![]() 1xzhC ![]() 1xziC ![]() 1xzjC ![]() 1xzkC ![]() 1xzlC ![]() 1xzmC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 22250.873 Da / Num. of mol.: 1 / Mutation: R196E Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#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: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 36 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / PH range low: 8 / PH range high: 6 | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 180 mm plate / Detector: IMAGE PLATE / 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 | Num. obs: 16320 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Rmerge(I) obs: 0.067 |
Reflection | *PLUS Highest resolution: 1.75 Å / Num. measured all: 75375 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.75→6 Å / σ(F): 1 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→6 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 37.2 Å2 |