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Yorodumi- PDB-1mot: NMR Structure Of Extended Second Transmembrane Domain Of Glycine ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mot | ||||||
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Title | NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles | ||||||
Components | Glycine Receptor alpha-1 CHAIN | ||||||
Keywords | MEMBRANE PROTEIN / glycine receptor / second transmembrane domain / micelles | ||||||
Function / homology | Function and homology information taurine binding / negative regulation of transmission of nerve impulse / Neurotransmitter receptors and postsynaptic signal transmission / acrosome reaction / positive regulation of acrosome reaction / synaptic transmission, glycinergic / neuromuscular process controlling posture / inhibitory synapse / regulation of respiratory gaseous exchange by nervous system process / righting reflex ...taurine binding / negative regulation of transmission of nerve impulse / Neurotransmitter receptors and postsynaptic signal transmission / acrosome reaction / positive regulation of acrosome reaction / synaptic transmission, glycinergic / neuromuscular process controlling posture / inhibitory synapse / regulation of respiratory gaseous exchange by nervous system process / righting reflex / extracellularly glycine-gated chloride channel activity / response to alcohol / glycinergic synapse / inhibitory postsynaptic potential / cellular response to ethanol / chloride transport / adult walking behavior / cellular response to zinc ion / neurotransmitter receptor activity / glycine binding / startle response / chloride channel complex / neuronal action potential / neuropeptide signaling pathway / transmembrane transporter complex / monoatomic ion transport / chloride transmembrane transport / muscle contraction / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / visual perception / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / cellular response to amino acid stimulus / transmembrane signaling receptor activity / perikaryon / postsynaptic membrane / neuron projection / external side of plasma membrane / intracellular membrane-bounded organelle / neuronal cell body / dendrite / synapse / zinc ion binding / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Yushmanov, V.E. / Mandal, P.K. / Liu, Z. / Tang, P. / Xu, Y. | ||||||
Citation | Journal: Biochemistry / Year: 2003 Title: NMR Structure and Backbone Dynamics of the Extended Second Transmembrane Domain of the Human Neuronal Glycine Receptor Alpha1 Subunit Authors: Yushmanov, V.E. / Mandal, P.K. / Liu, Z. / Tang, P. / Xu, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mot.cif.gz | 180.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mot.ent.gz | 151.4 KB | Display | PDB format |
PDBx/mmJSON format | 1mot.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mot_validation.pdf.gz | 334.8 KB | Display | wwPDB validaton report |
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Full document | 1mot_full_validation.pdf.gz | 427.2 KB | Display | |
Data in XML | 1mot_validation.xml.gz | 10.2 KB | Display | |
Data in CIF | 1mot_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mo/1mot ftp://data.pdbj.org/pub/pdb/validation_reports/mo/1mot | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2804.249 Da / Num. of mol.: 1 / Fragment: Extented second transmembrane domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GLRA1 / Plasmid: pGEX-3X / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P23415 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using standard 2D homonuclear and triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: SDS concentration: 300 mM Peptide concentration: 2 mM Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 300 mM SDS concentration / pH: 5 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 187 restraints, 169 are NOE-derived distance constraints,18 distance restraints from hydrogen bonds | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 20 |