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Yorodumi- PDB-1ffa: CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATIO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ffa | ||||||
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Title | CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO THE STABILIZATION OF THE OXYANION TRANSITION STATE | ||||||
Components | CUTINASE | ||||||
Keywords | HYDROLASE (SERINE ESTERASE) | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Nectria haematococca mpVI (fungus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.69 Å | ||||||
Authors | Cambillau, C. / Martinez, C. / Nicolas, A. | ||||||
Citation | 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. #1: 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. #2: 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 | 1ffa.cif.gz | 70 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ffa.ent.gz | 56.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ffa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ffa_validation.pdf.gz | 360.3 KB | Display | wwPDB validaton report |
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Full document | 1ffa_full_validation.pdf.gz | 360.3 KB | Display | |
Data in XML | 1ffa_validation.xml.gz | 5 KB | Display | |
Data in CIF | 1ffa_validation.cif.gz | 8.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ff/1ffa ftp://data.pdbj.org/pub/pdb/validation_reports/ff/1ffa | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 22322.043 Da / Num. of mol.: 1 / Mutation: N84A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Nectria haematococca mpVI (fungus) / Species: Nectria haematococca / Strain: mpVI / Description: ESCHERICHIA COLI CLONING SYSTEM / Plasmid: PUC 19 / Production host: Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P00590, triacylglycerol lipase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.17 % | ||||||||||||||||||||
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Crystal | *PLUS Density % sol: 38 % | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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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 / Date: Jan 15, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 18092 / % possible obs: 95.3 % / Observed criterion σ(I): 1 / Redundancy: 3.3 % / Rmerge(I) obs: 0.029 |
Reflection | *PLUS Highest resolution: 1.69 Å / Num. measured all: 60359 / Rmerge(I) obs: 0.029 |
-Processing
Software |
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Refinement | Resolution: 1.69→6 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 38.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.69→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 |