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Yorodumi- PDB-3te4: Crystal structure of dopamine N Acetyltransferase in complex with... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3te4 | ||||||
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Title | Crystal structure of dopamine N Acetyltransferase in complex with acetyl-COA from Drosophila Melanogaster | ||||||
Components | Dopamine N acetyltransferase, isoform A | ||||||
Keywords | TRANSFERASE / DOPAMINE/ACETYL COA / N-acetyltransferase domain | ||||||
Function / homology | Function and homology information chitin-based cuticle sclerotization / serotonin catabolic process / octopamine catabolic process / aralkylamine N-acetyltransferase / aralkylamine N-acetyltransferase activity / arylamine N-acetyltransferase activity / melatonin biosynthetic process / regulation of circadian sleep/wake cycle, sleep / catecholamine metabolic process / dopamine catabolic process ...chitin-based cuticle sclerotization / serotonin catabolic process / octopamine catabolic process / aralkylamine N-acetyltransferase / aralkylamine N-acetyltransferase activity / arylamine N-acetyltransferase activity / melatonin biosynthetic process / regulation of circadian sleep/wake cycle, sleep / catecholamine metabolic process / dopamine catabolic process / sleep / N-acetyltransferase activity / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.46 Å | ||||||
Authors | Cheng, K.C. / Huang, S.H. / Lyu, P.C. | ||||||
Citation | Journal: Biochem.J. / Year: 2012 Title: Crystal structure of the dopamine N-acetyltransferase-acetyl-CoA complex provides insights into the catalytic mechanism Authors: Cheng, K.C. / Liao, J.N. / Lyu, P.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3te4.cif.gz | 114.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3te4.ent.gz | 89.2 KB | Display | PDB format |
PDBx/mmJSON format | 3te4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/te/3te4 ftp://data.pdbj.org/pub/pdb/validation_reports/te/3te4 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 24442.049 Da / Num. of mol.: 1 / Fragment: UNP residues 21-230 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: CG3318, Dat, Dmel_CG3318 / Plasmid: PGEX-6P-3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q8MKK2, UniProt: Q94521*PLUS, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups, arylamine N-acetyltransferase, aralkylamine N-acetyltransferase |
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#2: Chemical | ChemComp-ACO / |
#3: 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: 2.14 Å3/Da / Density % sol: 42.54 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 1.0M NAH2PO4/1.6M K2HPO4, 0.1M IMIDAZOLE, 0.2M NACL , pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1 / Wavelength: 0.96369 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 23, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.96369 Å / Relative weight: 1 |
Reflection | Resolution: 1.46→30 Å / Num. obs: 36678 / % possible obs: 98.7 % / Redundancy: 5.5 % / Biso Wilson estimate: 19.1 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 23.4 |
Reflection shell | Resolution: 1.46→1.51 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.205 / Mean I/σ(I) obs: 9.25 / % possible all: 98.7 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.46→23.61 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.948 / SU B: 2.139 / SU ML: 0.038 / Cross valid method: THROUGHOUT / ESU R Free: 0.072 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.4 Å2
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Refinement step | Cycle: LAST / Resolution: 1.46→23.61 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.46→1.5 Å / Total num. of bins used: 20
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