+Open data
-Basic information
Entry | Database: PDB / ID: 6jxu | ||||||
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Title | SUMO1 bound to SLS4-SIM peptide from ICP0 | ||||||
Components |
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Keywords | PROTEIN BINDING/PEPTIDE / SUMOylation / PROTEIN BINDING-PEPTIDE complex | ||||||
Function / homology | Function and homology information symbiont-mediated perturbation of host exit from mitosis / release from viral latency / protein localization to nuclear pore / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / suppression by virus of host type I interferon production ...symbiont-mediated perturbation of host exit from mitosis / release from viral latency / protein localization to nuclear pore / negative regulation of transcription by transcription factor localization / SUMOylation of nuclear envelope proteins / Negative regulation of activity of TFAP2 (AP-2) family transcription factors / SUMO is proteolytically processed / negative regulation of delayed rectifier potassium channel activity / SUMO is conjugated to E1 (UBA2:SAE1) / suppression by virus of host type I interferon production / nuclear stress granule / PML body organization / viral tegument / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / positive regulation of ATPase-coupled calcium transmembrane transporter activity / negative regulation of action potential / small protein activating enzyme binding / septin ring / regulation of calcium ion transmembrane transport / SUMOylation of DNA methylation proteins / SUMOylation of immune response proteins / XY body / SUMOylation of SUMOylation proteins / response to type I interferon / Maturation of nucleoprotein / SUMOylation of RNA binding proteins / regulation of cardiac muscle cell contraction / Postmitotic nuclear pore complex (NPC) reformation / Maturation of nucleoprotein / symbiont-mediated disruption of host cell PML body / negative regulation of protein import into nucleus / ubiquitin-specific protease binding / roof of mouth development / SUMOylation of ubiquitinylation proteins / ubiquitin-like protein ligase binding / negative regulation of DNA binding / SUMOylation of DNA replication proteins / protein sumoylation / transcription factor binding / SUMOylation of transcription factors / potassium channel regulator activity / SUMOylation of DNA damage response and repair proteins / Regulation of IFNG signaling / nuclear pore / cellular response to cadmium ion / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / positive regulation of protein-containing complex assembly / SUMOylation of intracellular receptors / RING-type E3 ubiquitin transferase / PKR-mediated signaling / regulation of protein stability / negative regulation of DNA-binding transcription factor activity / PML body / Formation of Incision Complex in GG-NER / protein polyubiquitination / protein tag activity / positive regulation of protein catabolic process / ubiquitin-protein transferase activity / regulation of protein localization / ubiquitin protein ligase activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / cellular response to heat / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / symbiont-mediated perturbation of host ubiquitin-like protein modification / nuclear membrane / host cell cytoplasm / nuclear body / protein stabilization / nuclear speck / DNA repair / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / host cell nucleus / regulation of DNA-templated transcription / nucleolus / enzyme binding / DNA binding / RNA binding / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Human herpesvirus 1 (Herpes simplex virus type 1) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Hembram, D.S.S. / Negi, H. / Shet, D. / Das, R. | ||||||
Funding support | India, 1items
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Citation | Journal: J.Mol.Biol. / Year: 2020 Title: The Viral SUMO-Targeted Ubiquitin Ligase ICP0 is Phosphorylated and Activated by Host Kinase Chk2. Authors: Hembram, D.S.S. / Negi, H. / Biswas, P. / Tripathi, V. / Bhushan, L. / Shet, D. / Kumar, V. / Das, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6jxu.cif.gz | 560.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6jxu.ent.gz | 465.8 KB | Display | PDB format |
PDBx/mmJSON format | 6jxu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jx/6jxu ftp://data.pdbj.org/pub/pdb/validation_reports/jx/6jxu | HTTPS FTP |
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-Related structure data
Related structure data | 6jxvC 6jxwC 6jxxC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11575.005 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SUMO1 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A024R3Z2, UniProt: P63165*PLUS |
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#2: Protein/peptide | Mass: 1327.422 Da / Num. of mol.: 1 / Source method: obtained synthetically Source: (synth.) Human herpesvirus 1 (Herpes simplex virus type 1) References: UniProt: P08393*PLUS |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions |
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-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 6 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |