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- PDB-3ls2: Crystal structure of an S-formylglutathione hydrolase from Pseudo... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3ls2 | ||||||
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Title | Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125 | ||||||
![]() | S-formylglutathione Hydrolase | ||||||
![]() | HYDROLASE / S-formylglutathione hydrolase / psychrophilic organism / Pseudoalteromonas haloplanktis | ||||||
Function / homology | ![]() S-formylglutathione hydrolase / S-formylglutathione hydrolase activity / formaldehyde catabolic process / carboxylic ester hydrolase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Alterio, V. / De Simone, G. | ||||||
![]() | ![]() Title: Crystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125. Authors: Alterio, V. / Aurilia, V. / Romanelli, A. / Parracino, A. / Saviano, M. / D'Auria, S. / De Simone, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 243.6 KB | Display | ![]() |
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PDB format | ![]() | 194.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446 KB | Display | ![]() |
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Full document | ![]() | 455.2 KB | Display | |
Data in XML | ![]() | 51.1 KB | Display | |
Data in CIF | ![]() | 75 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1pv1S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 30915.732 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: TAC125 / Gene: PSHAa1385 / Plasmid: pET28a / Production host: ![]() ![]() References: UniProt: Q3IL66, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases #2: Chemical | ChemComp-CL / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37.94 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 20% (w/v) PEG MME 5000, 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293 K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944 / Detector: CCD / Date: Jul 10, 2009 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. all: 49990 / Num. obs: 49990 / % possible obs: 98.7 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.053 / Net I/σ(I): 19.5 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.166 / Mean I/σ(I) obs: 5.9 / Num. unique all: 4666 / % possible all: 93.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1PV1 Resolution: 2.2→20 Å / Isotropic thermal model: isotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 15.6 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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