+Open data
-Basic information
Entry | Database: PDB / ID: 8as4 | ||||||
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Title | Crystal structure of human beta-arrestin-1 | ||||||
Components | Beta-arrestin-1Arrestin | ||||||
Keywords | SIGNALING PROTEIN / Arrestin / GPCR | ||||||
Function / homology | Function and homology information angiotensin receptor binding / Activation of SMO / negative regulation of interleukin-8 production / arrestin family protein binding / G protein-coupled receptor internalization / enzyme inhibitor activity / Lysosome Vesicle Biogenesis / positive regulation of Rho protein signal transduction / Golgi Associated Vesicle Biogenesis / negative regulation of NF-kappaB transcription factor activity ...angiotensin receptor binding / Activation of SMO / negative regulation of interleukin-8 production / arrestin family protein binding / G protein-coupled receptor internalization / enzyme inhibitor activity / Lysosome Vesicle Biogenesis / positive regulation of Rho protein signal transduction / Golgi Associated Vesicle Biogenesis / negative regulation of NF-kappaB transcription factor activity / stress fiber assembly / negative regulation of Notch signaling pathway / pseudopodium / negative regulation of interleukin-6 production / positive regulation of receptor internalization / clathrin-coated pit / negative regulation of protein ubiquitination / insulin-like growth factor receptor binding / visual perception / Activated NOTCH1 Transmits Signal to the Nucleus / GTPase activator activity / G protein-coupled receptor binding / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / cytoplasmic vesicle membrane / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / Thrombin signalling through proteinase activated receptors (PARs) / protein transport / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / ubiquitin-dependent protein catabolic process / G alpha (s) signalling events / cytoplasmic vesicle / proteasome-mediated ubiquitin-dependent protein catabolic process / transcription coactivator activity / positive regulation of ERK1 and ERK2 cascade / protein ubiquitination / nuclear body / Ub-specific processing proteases / positive regulation of protein phosphorylation / lysosomal membrane / Golgi membrane / ubiquitin protein ligase binding / chromatin / regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Jakob, R.P. / Panwalkar, V. / Grzesiek, S. | ||||||
Funding support | Switzerland, 1items
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Citation | Journal: Mol.Cell / Year: 2023 Title: A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes. Authors: Isaikina, P. / Petrovic, I. / Jakob, R.P. / Sarma, P. / Ranjan, A. / Baruah, M. / Panwalkar, V. / Maier, T. / Shukla, A.K. / Grzesiek, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8as4.cif.gz | 558.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8as4.ent.gz | 466.4 KB | Display | PDB format |
PDBx/mmJSON format | 8as4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/8as4 ftp://data.pdbj.org/pub/pdb/validation_reports/as/8as4 | HTTPS FTP |
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-Related structure data
Related structure data | 8as2C 8as3C 1g4mS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 47119.500 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARRB1, ARR1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P49407 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.17 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.02 M Calcium chloride 0.02 M Cadmium chloride hydrate, 0.02 M Cobalt(II) chloride hexahydrate, 20%PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.999999 Å |
Detector | Type: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Sep 14, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.999999 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→44.98 Å / Num. obs: 44486 / % possible obs: 100 % / Redundancy: 27.1 % / CC1/2: 0.99 / Rmerge(I) obs: 0.24 / Rpim(I) all: 0.07 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 27 % / Rmerge(I) obs: 2.46 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 4409 / CC1/2: 0.79 / Rpim(I) all: 0.78 / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1G4M Resolution: 2.3→44.98 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.922 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.25 / SU Rfree Blow DPI: 0.192
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Displacement parameters | Biso max: 237.06 Å2 / Biso mean: 80.42 Å2 / Biso min: 25.4 Å2
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Refine analyze | Luzzati coordinate error obs: 0.37 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.3→44.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.32 Å / Rfactor Rfree error: 0 / Total num. of bins used: 50
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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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