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Yorodumi- PDB-1t1u: Structural Insights and Functional Implications of Choline Acetyl... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1t1u | ||||||
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Title | Structural Insights and Functional Implications of Choline Acetyltransferase | ||||||
Components | Choline O-acetyltransferase | ||||||
Keywords | TRANSFERASE / choline acetyltransferase | ||||||
Function / homology | Function and homology information choline O-acetyltransferase / choline O-acetyltransferase activity / Synthesis of PC / acetylcholine biosynthetic process / rhythmic excitation / establishment of synaptic specificity at neuromuscular junction / rhythmic behavior / Acetylcholine Neurotransmitter Release Cycle / neuromuscular synaptic transmission / choline binding ...choline O-acetyltransferase / choline O-acetyltransferase activity / Synthesis of PC / acetylcholine biosynthetic process / rhythmic excitation / establishment of synaptic specificity at neuromuscular junction / rhythmic behavior / Acetylcholine Neurotransmitter Release Cycle / neuromuscular synaptic transmission / choline binding / adult walking behavior / muscle organ development / antral ovarian follicle growth / dendrite development / response to nutrient / neuron differentiation / memory / chemical synaptic transmission / response to ethanol / response to hypoxia / neuron projection / response to xenobiotic stimulus / axon / neuronal cell body / synapse / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||
Authors | Govindasamy, L. / Pedersen, B. / Lian, W. / Kukar, T. / Gu, Y. / Jin, S. / Agbandje-McKenna, M. / Wu, D. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2004 Title: Structural insights and functional implications of choline acetyltransferase Authors: Govindasamy, L. / Pedersen, B. / Lian, W. / Kukar, T. / Gu, Y. / Jin, S. / Agbandje-McKenna, M. / Wu, D. | ||||||
History |
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Remark 999 | SEQUENCE The author states that the database reference sequence used in this structure contains errors. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t1u.cif.gz | 154.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t1u.ent.gz | 109.9 KB | Display | PDB format |
PDBx/mmJSON format | 1t1u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t1/1t1u ftp://data.pdbj.org/pub/pdb/validation_reports/t1/1t1u | HTTPS FTP |
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-Related structure data
Related structure data | 1nm8S S: Starting model for refinement |
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Similar 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: 71905.500 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Chat / Production host: Escherichia coli (E. coli) / References: UniProt: P32738, choline O-acetyltransferase |
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#2: 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: 2.22 Å3/Da / Density % sol: 44.52 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 50mM MES buffer, 100mM NaCl, PEG 8000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.9504 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9504 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→30 Å / Num. all: 429316 / Num. obs: 72446 / Biso Wilson estimate: 26.9 Å2 / Rsym value: 0.054 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 1.51→1.55 Å / Mean I/σ(I) obs: 3.2 / Num. unique all: 72446 / Rsym value: 0.337 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1NM8 Resolution: 1.55→30 Å / Isotropic thermal model: isotropic / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 23.814 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→30 Å
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Refine LS restraints |
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