+Open data
-Basic information
Entry | Database: PDB / ID: 1xz9 | ||||||
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Title | Structure of AF-6 PDZ domain | ||||||
Components | Afadin | ||||||
Keywords | CELL ADHESION / PDZ / AF-6 | ||||||
Function / homology | Function and homology information positive regulation of cell-cell adhesion mediated by cadherin / establishment of protein localization to plasma membrane / : / establishment of endothelial intestinal barrier / positive regulation of cell-cell adhesion / pore complex assembly / cell-cell adhesion mediated by cadherin / bicellular tight junction assembly / cell-cell contact zone / Adherens junctions interactions ...positive regulation of cell-cell adhesion mediated by cadherin / establishment of protein localization to plasma membrane / : / establishment of endothelial intestinal barrier / positive regulation of cell-cell adhesion / pore complex assembly / cell-cell adhesion mediated by cadherin / bicellular tight junction assembly / cell-cell contact zone / Adherens junctions interactions / tight junction / pore complex / cell adhesion molecule binding / negative regulation of cell migration / adherens junction / small GTPase binding / positive regulation of GTPase activity / regulation of protein localization / actin filament binding / cell-cell junction / cell-cell signaling / cell junction / cell adhesion / nuclear speck / cadherin binding / positive regulation of gene expression / signal transduction / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Joshi, M. / Boisguerin, P. / Leitner, D. / Volkmer-Engert, R. / Moelling, K. / Schade, M. / Schmieder, P. / Krause, G. / Oschkinat, H. | ||||||
Citation | Journal: Angew.Chem.Int.Ed.Engl. / Year: 2006 Title: Discovery of low-molecular-weight ligands for the AF6 PDZ domain. Authors: Joshi, M. / Vargas, C. / Boisguerin, P. / Diehl, A. / Krause, G. / Schmieder, P. / Moelling, K. / Hagen, V. / Schade, M. / Oschkinat, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xz9.cif.gz | 580.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xz9.ent.gz | 499.2 KB | Display | PDB format |
PDBx/mmJSON format | 1xz9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xz/1xz9 ftp://data.pdbj.org/pub/pdb/validation_reports/xz/1xz9 | 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: 10392.987 Da / Num. of mol.: 1 / Fragment: AF-6 PDZ domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q5TIG6, UniProt: P55196*PLUS |
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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 triple-resonance NMR spectroscopy |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 20mM Phosphate, 50mM Sodium Chloride / pH: 7.0 / Pressure: Ambient / Temperature: 295 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 |