+Open data
-Basic information
Entry | Database: PDB / ID: 1xzk | ||||||
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Title | FUSARIUM SOLANI CUTINASE COMPLEX WITH DI(ISOPROPYL)PHOSPHATE | ||||||
Components | CUTINASE | ||||||
Keywords | HYDROLASE (SERINE ESTERASE) / HYDROLASE / SERINE ESTERASE / GLYCOPROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Nectria haematococca mpVI (fungus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.01 Å | ||||||
Authors | Martinez, C. / Cambillau, C. | ||||||
Citation | Journal: Proteins / Year: 1996 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: Journal: Biochemistry / Year: 1996 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. #2: Journal: Biochemistry / Year: 1994 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: Journal: Nature / Year: 1992 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xzk.cif.gz | 108.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xzk.ent.gz | 88.7 KB | Display | PDB format |
PDBx/mmJSON format | 1xzk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xz/1xzk ftp://data.pdbj.org/pub/pdb/validation_reports/xz/1xzk | HTTPS FTP |
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-Related structure data
Related structure data | 1cuaC 1cubC 1cucC 1cudC 1cueC 1cufC 1cugC 1cuhC 1cuiC 1cujC 1cuuC 1cuvC 1cuwC 1cuxC 1cuyC 1cuzC 1xzaC 1xzdC 1xzeC 1xzfC 1xzgC 1xzhC 1xziC 1xzjC 1xzlC 1xzmC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.89788, 0.08634, 0.43169), Vector: |
-Components
#1: Protein | Mass: 22351.016 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: COMPLEX WITH DI(ISOPROPYL)PHOSPHATE / Source: (gene. exp.) Nectria haematococca mpVI (fungus) / Species: Nectria haematococca / Strain: mpVI / Plasmid: PUC 19 / Production host: Escherichia coli (E. coli) References: UniProt: P00590, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases #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 | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 43 % | |||||||||||||||||||||||||
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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 source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / 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: 22117 / % possible obs: 90 % / Observed criterion σ(I): 0 / Redundancy: 2.66 % / Rmerge(I) obs: 0.046 |
Reflection | *PLUS Highest resolution: 2.01 Å / Num. measured all: 52036 |
-Processing
Software |
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Refinement | Resolution: 2.01→6 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 2.01→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |