+Open data
-Basic information
Entry | Database: PDB / ID: 5kk9 | ||||||
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Title | Connexin 32 G12R N-Terminal Mutant, | ||||||
Components | Gap junction beta-1 protein | ||||||
Keywords | TRANSPORT PROTEIN / Connexin 32 G12R N-Terminal Mutant | ||||||
Function / homology | Function and homology information purine ribonucleotide transport / epididymis development / Oligomerization of connexins into connexons / Transport of connexins along the secretory pathway / gap junction assembly / connexin complex / Gap junction assembly / gap junction channel activity / lateral plasma membrane / cell-cell signaling ...purine ribonucleotide transport / epididymis development / Oligomerization of connexins into connexons / Transport of connexins along the secretory pathway / gap junction assembly / connexin complex / Gap junction assembly / gap junction channel activity / lateral plasma membrane / cell-cell signaling / nervous system development / endoplasmic reticulum membrane / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Dowd, T.L. / Barigello, T.A. | ||||||
Funding support | United States, 1items
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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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5kk9.cif.gz | 132.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5kk9.ent.gz | 105.5 KB | Display | PDB format |
PDBx/mmJSON format | 5kk9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kk/5kk9 ftp://data.pdbj.org/pub/pdb/validation_reports/kk/5kk9 | 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/peptide | Mass: 2576.977 Da / Num. of mol.: 1 / Mutation: G12R / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P08034 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 1.0 mM ACE-MET-ASN-TRP-THR-GLY-LEU-TYR-THR-LEU-LEU-SER-ARG-VAL-ASN-ARG-HIS-SER-THR-ALA-ILE-GLY-ARG, 100 mM KCl, 100 uM TSP, 90% H2O/10% D2O Details: 1.0 mM Cx32 G12R N-terminal peptide dissolved in 0.1M KCl. Label: 1H_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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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 |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 5 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformers submitted total number: 20 |