+Open data
-Basic information
Entry | Database: PDB / ID: 5kjg | ||||||
---|---|---|---|---|---|---|---|
Title | Connexin 26 G12R mutant NMR structure | ||||||
Components | Gap junction beta-2 protein | ||||||
Keywords | TRANSPORT PROTEIN / Connexin 26 G12R Mutant | ||||||
Function / homology | Function and homology information Transport of connexons to the plasma membrane / response to human chorionic gonadotropin / gap junction-mediated intercellular transport / epididymis development / gap junction channel activity involved in cell communication by electrical coupling / Oligomerization of connexins into connexons / Transport of connexins along the secretory pathway / gap junction assembly / connexin complex / Gap junction assembly ...Transport of connexons to the plasma membrane / response to human chorionic gonadotropin / gap junction-mediated intercellular transport / epididymis development / gap junction channel activity involved in cell communication by electrical coupling / Oligomerization of connexins into connexons / Transport of connexins along the secretory pathway / gap junction assembly / connexin complex / Gap junction assembly / astrocyte projection / gap junction channel activity / gap junction / cellular response to glucagon stimulus / inner ear development / decidualization / endoplasmic reticulum-Golgi intermediate compartment / lateral plasma membrane / response to retinoic acid / cellular response to dexamethasone stimulus / response to progesterone / response to ischemia / sensory perception of sound / transmembrane transport / response to estradiol / cell-cell signaling / cellular response to oxidative stress / cell body / response to lipopolysaccharide / calcium ion binding / perinuclear region of cytoplasm / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Dowd, T.L. / Bargiello, T.A. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: Arch.Biochem.Biophys. / Year: 2016 Title: Structural studies of N-terminal mutants of Connexin 26 and Connexin 32 using (1)H NMR spectroscopy. Authors: Batir, Y. / Bargiello, T.A. / Dowd, T.L. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5kjg.cif.gz | 128.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5kjg.ent.gz | 102.2 KB | Display | PDB format |
PDBx/mmJSON format | 5kjg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kj/5kjg ftp://data.pdbj.org/pub/pdb/validation_reports/kj/5kjg | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein/peptide | Mass: 2472.863 Da / Num. of mol.: 1 / Mutation: G12R / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P29033 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Type: solution Contents: 1.0 mM NA ACE-MET-ASP-TRP-GLY-THR-LEU-GLN-THR-ILE-LEU-GLY-ARG-VAL-ASN-LYS-HIS-SER-THR-SER-ILE-GLY-LYS, 100 mM KCL, 100 uM TSP, 90% H2O/10% D2O Details: Connexin 26 G12R mutant peptide dissolved in 0.1 M KCl solution Label: 1H_Cx26G12R sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||
Sample conditions | Ionic strength: 0.1 M / Ionic strength err: 0.01 / Label: conditions_1 / pH: 7.0 / PH err: 0.05 / Pressure: 1 atm / Pressure err: 0.01 / Temperature: 288 K / Temperature err: 0.2 |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 4 | |||||||||||||||
NMR representative | Selection criteria: low energy | |||||||||||||||
NMR ensemble | Conformers submitted total number: 20 |