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Yorodumi- PDB-2m6b: Structure of full-length transmembrane domains of human glycine r... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2m6b | ||||||
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Title | Structure of full-length transmembrane domains of human glycine receptor alpha1 monomer subunit | ||||||
Components | Full-Length Transmembrane Domains of Human Glycine Receptor alpha1 Subunit | ||||||
Keywords | MEMBRANE PROTEIN / glycine receptor / anion channel / transmembrane domain | ||||||
Function / homology | Function and homology information taurine binding / response to alcohol / negative regulation of transmission of nerve impulse / Neurotransmitter receptors and postsynaptic signal transmission / positive regulation of acrosome reaction / acrosome reaction / neuromuscular process controlling posture / inhibitory synapse / righting reflex / regulation of respiratory gaseous exchange by nervous system process ...taurine binding / response to alcohol / negative regulation of transmission of nerve impulse / Neurotransmitter receptors and postsynaptic signal transmission / positive regulation of acrosome reaction / acrosome reaction / neuromuscular process controlling posture / inhibitory synapse / righting reflex / regulation of respiratory gaseous exchange by nervous system process / extracellularly glycine-gated chloride channel activity / synaptic transmission, glycinergic / glycinergic synapse / inhibitory postsynaptic potential / cellular response to ethanol / adult walking behavior / chloride transport / cellular response to zinc ion / glycine binding / startle response / chloride channel complex / neuropeptide signaling pathway / neuronal action potential / response to amino acid / monoatomic ion transport / chloride transmembrane transport / 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 / muscle contraction / cellular response to amino acid stimulus / transmembrane signaling receptor activity / postsynaptic membrane / perikaryon / neuron projection / external side of plasma membrane / intracellular membrane-bounded organelle / neuronal cell body / synapse / dendrite / zinc ion binding / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Mowrey, D. / Cui, T. / Jia, Y. / Ma, D. / Makhov, A.M. / Zhang, P. / Tang, P. / Xu, Y. | ||||||
Citation | Journal: Structure / Year: 2013 Title: Open-Channel Structures of the Human Glycine Receptor alpha 1 Full-Length Transmembrane Domain. Authors: Mowrey, D.D. / Cui, T. / Jia, Y. / Ma, D. / Makhov, A.M. / Zhang, P. / 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 | 2m6b.cif.gz | 827.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m6b.ent.gz | 705.4 KB | Display | PDB format |
PDBx/mmJSON format | 2m6b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m6/2m6b ftp://data.pdbj.org/pub/pdb/validation_reports/m6/2m6b | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17320.320 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET-31b(+) / Production host: Escherichia coli (E. coli) / References: UniProt: P23415*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 280 uM protein, 95% H2O/5% D2O / Solvent system: 95% H2O/5% D2O |
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Sample | Conc.: 280 uM / Component: protein-1 |
Sample conditions | pH: 5.8 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software | Name: CYANA / Version: 3 / Developer: Guntert, P. et al. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR constraints | NOE constraints total: 1014 / NOE intraresidue total count: 321 / NOE long range total count: 21 / NOE medium range total count: 324 / NOE sequential total count: 348 / Hydrogen bond constraints total count: 212 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 219 / Protein phi angle constraints total count: 76 / Protein psi angle constraints total count: 76 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Average torsion angle constraint violation: 0.13 ° / Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 15 / Maximum torsion angle constraint violation: 1.29 ° / Maximum upper distance constraint violation: 0.24 Å |