+Open data
-Basic information
Entry | Database: PDB / ID: 4mob | ||||||
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Title | Acyl-Coenzyme A thioesterase 12 in complex with ADP | ||||||
Components | Acyl-coenzyme A thioesterase 12 | ||||||
Keywords | HYDROLASE / Hotdog / ACOT12 / CACH / STARD15 | ||||||
Function / homology | Function and homology information acetyl-CoA hydrolase / acetyl-CoA hydrolase activity / acyl-CoA metabolic process / acetyl-CoA metabolic process / fatty acyl-CoA hydrolase activity / Mitochondrial Fatty Acid Beta-Oxidation / carboxylic ester hydrolase activity / intercellular bridge / fatty acid metabolic process / lipid binding ...acetyl-CoA hydrolase / acetyl-CoA hydrolase activity / acyl-CoA metabolic process / acetyl-CoA metabolic process / fatty acyl-CoA hydrolase activity / Mitochondrial Fatty Acid Beta-Oxidation / carboxylic ester hydrolase activity / intercellular bridge / fatty acid metabolic process / lipid binding / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.401 Å | ||||||
Authors | Swarbrick, C.M.D. / Forwood, J.K. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2014 Title: Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain. Authors: Swarbrick, C.M. / Roman, N. / Cowieson, N. / Patterson, E.I. / Nanson, J. / Siponen, M.I. / Berglund, H. / Lehtio, L. / Forwood, J.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mob.cif.gz | 81 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mob.ent.gz | 59.8 KB | Display | PDB format |
PDBx/mmJSON format | 4mob.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mo/4mob ftp://data.pdbj.org/pub/pdb/validation_reports/mo/4mob | HTTPS FTP |
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-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: 37111.441 Da / Num. of mol.: 1 / Fragment: UNP residues 7-336 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACOT12, CACH, CACH1, STARD15 / Plasmid: PNIC-Bsa4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) pLysS / References: UniProt: Q8WYK0, acetyl-CoA hydrolase |
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#2: Chemical | ChemComp-COA / |
#3: Chemical | ChemComp-ADP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.01 Å3/Da / Density % sol: 59.07 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop Details: 275 mM potassium phosphate dibasic, 12.5% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 296K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 5, 2013 |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→34.712 Å / Num. obs: 17555 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Net I/σ(I): 2.6 |
Reflection shell | Resolution: 2.4→2.51 Å / Redundancy: 21.8 % / Rmerge(I) obs: 1.344 / Mean I/σ(I) obs: 2.6 / Num. unique all: 2114 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.401→34.712 Å / SU ML: 0.33 / σ(F): 1.35 / Phase error: 21.45 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.401→34.712 Å
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Refine LS restraints |
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LS refinement shell |
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