+Open data
-Basic information
Entry | Database: PDB / ID: 6a9x | ||||||
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Title | Crystal Structure of AnkG/GABARAP Complex | ||||||
Components |
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Keywords | PROTEIN BINDING / STRUCTURAL PROTEIN / SIGNALING PROTEIN | ||||||
Function / homology | Function and homology information positive regulation of sodium ion import across plasma membrane / positive regulation of cell communication by electrical coupling / positive regulation of membrane depolarization during cardiac muscle cell action potential / regulation of protein targeting / maintenance of protein location in plasma membrane / membrane assembly / TBC/RABGAPs / Macroautophagy / protein localization to axon / clustering of voltage-gated sodium channels ...positive regulation of sodium ion import across plasma membrane / positive regulation of cell communication by electrical coupling / positive regulation of membrane depolarization during cardiac muscle cell action potential / regulation of protein targeting / maintenance of protein location in plasma membrane / membrane assembly / TBC/RABGAPs / Macroautophagy / protein localization to axon / clustering of voltage-gated sodium channels / positive regulation of sodium ion transmembrane transporter activity / establishment or maintenance of microtubule cytoskeleton polarity / regulation of potassium ion transport / spectrin-associated cytoskeleton / magnesium ion homeostasis / positive regulation of protein K48-linked ubiquitination / positive regulation of membrane potential / negative regulation of delayed rectifier potassium channel activity / plasma membrane organization / phosphorylation-dependent protein binding / positive regulation of homotypic cell-cell adhesion / positive regulation of cation channel activity / maintenance of protein location in cell / regulation of Rac protein signal transduction / axon initial segment / GABA receptor binding / paranode region of axon / positive regulation of sodium ion transport / Golgi to plasma membrane protein transport / negative regulation of endocytosis / node of Ranvier / costamere / cellular response to magnesium ion / phosphatidylethanolamine binding / regulation of modification of postsynaptic structure / anterograde axonal transport / cellular response to nitrogen starvation / microtubule associated complex / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / spectrin binding / neuromuscular junction development / axon development / beta-tubulin binding / axoneme / autophagosome membrane / autophagosome maturation / mitotic cytokinesis / intercalated disc / neuronal action potential / response to immobilization stress / extrinsic apoptotic signaling pathway via death domain receptors / autophagosome assembly / autophagosome / lateral plasma membrane / positive regulation of protein targeting to membrane / smooth endoplasmic reticulum / GABA-ergic synapse / axon cytoplasm / sperm midpiece / T-tubule / cytoskeletal protein binding / axonogenesis / basal plasma membrane / sarcoplasmic reticulum / axon guidance / protein localization to plasma membrane / synapse organization / establishment of protein localization / neuromuscular junction / structural constituent of cytoskeleton / sarcolemma / Z disc / microtubule cytoskeleton organization / positive regulation of non-canonical NF-kappaB signal transduction / actin cytoskeleton / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / protein transport / protein-macromolecule adaptor activity / cell body / cytoplasmic vesicle / microtubule binding / basolateral plasma membrane / postsynaptic membrane / RNA polymerase II-specific DNA-binding transcription factor binding / transmembrane transporter binding / postsynapse / microtubule / lysosome / cytoskeleton / neuron projection / cadherin binding / Golgi membrane / axon / glutamatergic synapse / ubiquitin protein ligase binding / synapse / dendrite / positive regulation of gene expression / regulation of transcription by RNA polymerase II / perinuclear region of cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.202 Å | ||||||
Authors | Wang, C. / Li, J. / Chen, K. / Zhang, M. | ||||||
Funding support | Hong Kong, 1items
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Citation | Journal: Mol. Psychiatry / Year: 2018 Title: Ankyrin-G regulates forebrain connectivity and network synchronization via interaction with GABARAP. Authors: Nelson, A.D. / Caballero-Floran, R.N. / Rodriguez Diaz, J.C. / Hull, J.M. / Yuan, Y. / Li, J. / Chen, K. / Walder, K.K. / Lopez-Santiago, L.F. / Bennett, V. / McInnis, M.G. / Isom, L.L. / ...Authors: Nelson, A.D. / Caballero-Floran, R.N. / Rodriguez Diaz, J.C. / Hull, J.M. / Yuan, Y. / Li, J. / Chen, K. / Walder, K.K. / Lopez-Santiago, L.F. / Bennett, V. / McInnis, M.G. / Isom, L.L. / Wang, C. / Zhang, M. / Jones, K.S. / Jenkins, P.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6a9x.cif.gz | 71.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6a9x.ent.gz | 51.9 KB | Display | PDB format |
PDBx/mmJSON format | 6a9x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a9/6a9x ftp://data.pdbj.org/pub/pdb/validation_reports/a9/6a9x | HTTPS FTP |
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-Related structure data
Related structure data | 1kjtS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13942.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Gabarap / Production host: Escherichia coli (E. coli) / References: UniProt: Q9DCD6 |
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#2: Protein/peptide | Mass: 2693.770 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ank3 / Production host: Escherichia coli (E. coli) / References: UniProt: O70511 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.18 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion / pH: 7 Details: 2.0 M ammonium citrate tribasic, 0.1 M BIS-TRIS propane buffer |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97853 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 20, 2015 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97853 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.2→50 Å / Num. obs: 7843 / % possible obs: 99.9 % / Redundancy: 19.6 % / Biso Wilson estimate: 26.93 Å2 / Rmerge(I) obs: 0.069 / Rpim(I) all: 0.017 / Rrim(I) all: 0.071 / Χ2: 0.993 / Net I/σ(I): 8.5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1KJT Resolution: 2.202→30.671 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 26.76
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 89.03 Å2 / Biso mean: 34.1556 Å2 / Biso min: 10.65 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.202→30.671 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 2
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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