+Open data
-Basic information
Entry | Database: PDB / ID: 5xht | ||||||
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Title | The PHD finger of human Kiaa1045 protein | ||||||
Components | PHD finger protein 24 | ||||||
Keywords | METAL BINDING PROTEIN / PHD finger / Zinc Finger | ||||||
Function / homology | Function and homology information regulation of G protein-coupled receptor signaling pathway / gamma-aminobutyric acid signaling pathway / regulation of synaptic transmission, GABAergic / detection of mechanical stimulus involved in sensory perception of pain / transcription corepressor activity / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Miyamoto, K. | ||||||
Citation | Journal: Protein Sci. / Year: 2018 Title: Solution structure of the PHD finger from the human KIAA1045 protein Authors: Miyamoto, K. / Yamashita, A. / Saito, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xht.cif.gz | 350.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xht.ent.gz | 300.1 KB | Display | PDB format |
PDBx/mmJSON format | 5xht.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xh/5xht ftp://data.pdbj.org/pub/pdb/validation_reports/xh/5xht | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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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 | Mass: 6858.710 Da / Num. of mol.: 1 / Fragment: UNP residues 131-190 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9UPV7 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Sample state: isotropic / Type: 3D NOESY |
-Sample preparation
Details | Type: solution / Contents: 1 mM U-13C;15N PHD finger, 90% H2O/10% D2O / Details: 20 mM Tris-HCl buffer, 50 mM NaCl, 1 mM DTT / Label: 13C 15N / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: PHD finger / Isotopic labeling: U-13C;15N |
Sample conditions | Ionic strength: 70 mM / Label: conditions_1 / pH: 6.9 / Pressure: 1 atm / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 3 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |