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- PDB-1c8u: CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF T... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c8u | ||||||
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Title | CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME | ||||||
![]() | ACYL-COA THIOESTERASE II | ||||||
![]() | HYDROLASE / INTERNAL REPEATS | ||||||
Function / homology | ![]() acyl-CoA metabolic process / fatty acyl-CoA hydrolase activity / fatty acid catabolic process / Hydrolases; Acting on ester bonds; Thioester hydrolases / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Li, J. / Derewenda, Z.S. | ||||||
![]() | ![]() Title: Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Authors: Li, J. / Derewenda, U. / Dauter, Z. / Smith, S. / Derewenda, Z.S. #1: ![]() Title: Crystallization of Thioesterase II from Escherichia Coli Authors: Swenson, L. / Green, R. / Smith, S. / Derewenda, Z.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 134.8 KB | Display | ![]() |
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PDB format | ![]() | 105.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.5 KB | Display | ![]() |
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Full document | ![]() | 454.9 KB | Display | |
Data in XML | ![]() | 30.7 KB | Display | |
Data in CIF | ![]() | 44 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 31873.062 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P23911, UniProt: P0AGG2*PLUS, Hydrolases; Acting on ester bonds; Thioester hydrolases #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.73 Å3/Da / Density % sol: 66.99 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: NACL, NAOAC, LDAO, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 10, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9096 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. all: 74901 / Num. obs: 74732 / % possible obs: 99.8 % / Observed criterion σ(I): 1 / Redundancy: 4.7 % / Biso Wilson estimate: 24 Å2 / Rmerge(I) obs: 0.059 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.425 / % possible all: 99.4 |
Reflection | *PLUS Num. obs: 74901 / % possible obs: 99.7 % / Num. measured all: 353158 |
Reflection shell | *PLUS % possible obs: 99.4 % |
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Processing
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Refinement | Resolution: 1.9→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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Software | *PLUS Name: 'CNS' / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.248 / Rfactor Rwork: 0.218 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |