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Yorodumi- PDB-6hmv: Crystal structure of human ACBD3 GOLD domain in complex with 3A p... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6hmv | ||||||
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| Title | Crystal structure of human ACBD3 GOLD domain in complex with 3A protein of enterovirus-D68 (fusion protein, LVVY mutant) | ||||||
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Keywords | VIRAL PROTEIN / complex / Golgi / enterovirus / picornavirus | ||||||
| Function / homology | Function and homology informationfatty-acyl-CoA binding / symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway / steroid biosynthetic process / Golgi Associated Vesicle Biogenesis / protein kinase A regulatory subunit binding / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / protein sequestering activity / ribonucleoside triphosphate phosphatase activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus ...fatty-acyl-CoA binding / symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway / steroid biosynthetic process / Golgi Associated Vesicle Biogenesis / protein kinase A regulatory subunit binding / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / protein sequestering activity / ribonucleoside triphosphate phosphatase activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / symbiont-mediated suppression of host toll-like receptor signaling pathway / symbiont-mediated suppression of host NF-kappaB cascade / RNA helicase activity / symbiont-mediated suppression of host innate immune response / endocytosis involved in viral entry into host cell / Golgi membrane / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / virion attachment to host cell / host cell nucleus / structural molecule activity / Golgi apparatus / ATP hydrolysis activity / mitochondrion / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) Enterovirus D68 | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.244 Å | ||||||
Authors | Klima, M. / Boura, E. | ||||||
| Funding support | Czech Republic, 1items
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Citation | Journal: Plos Pathog. / Year: 2019Title: Convergent evolution in the mechanisms of ACBD3 recruitment to picornavirus replication sites. Authors: Horova, V. / Lyoo, H. / Rozycki, B. / Chalupska, D. / Smola, M. / Humpolickova, J. / Strating, J.R.P.M. / van Kuppeveld, F.J.M. / Boura, E. / Klima, M. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6hmv.cif.gz | 49.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6hmv.ent.gz | 33.1 KB | Display | PDB format |
| PDBx/mmJSON format | 6hmv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6hmv_validation.pdf.gz | 415.4 KB | Display | wwPDB validaton report |
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| Full document | 6hmv_full_validation.pdf.gz | 415.3 KB | Display | |
| Data in XML | 6hmv_validation.xml.gz | 7.7 KB | Display | |
| Data in CIF | 6hmv_validation.cif.gz | 9.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hm/6hmv ftp://data.pdbj.org/pub/pdb/validation_reports/hm/6hmv | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6hlnC ![]() 6hltC ![]() 6hlvC ![]() 6hlwC ![]() 6hm8C ![]() 5lz1S S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 19389.346 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACBD3, GCP60, GOCAP1, GOLPH1 / Production host: ![]() |
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| #2: Protein/peptide | Mass: 5320.866 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterovirus D68 / Production host: ![]() References: UniProt: A0A2K9Y515, UniProt: Q68T42*PLUS, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.82 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, 30 mM MgCl2, 30 mM CaCl2, 100 mM bicine/Tris pH 8.5 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å |
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 18, 2018 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
| Reflection | Resolution: 2.244→40.45 Å / Num. obs: 13960 / % possible obs: 99.24 % / Redundancy: 7.1 % / Biso Wilson estimate: 49.92 Å2 / CC1/2: 0.995 / Rmerge(I) obs: 0.08654 / Rrim(I) all: 0.09373 / Net I/σ(I): 12.81 |
| Reflection shell | Resolution: 2.244→2.324 Å / Redundancy: 6.9 % / Rmerge(I) obs: 1.082 / Mean I/σ(I) obs: 1.52 / Num. unique obs: 1332 / CC1/2: 0.75 / % possible all: 95.42 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 5LZ1 Resolution: 2.244→40.45 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 33.49
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.244→40.45 Å
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| Refine LS restraints |
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| LS refinement shell |
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About Yorodumi



Homo sapiens (human)
Enterovirus D68
X-RAY DIFFRACTION
Czech Republic, 1items
Citation















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