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Open data
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Basic information
| Entry | Database: PDB / ID: 6kg6 | ||||||
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| Title | Crystal structure of MavC/UBE2N-Ub complex | ||||||
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Keywords | HYDROLASE/TRANSFERASE / complex / deamidase / ubiquitin / HYDROLASE / HYDROLASE-TRANSFERASE complex | ||||||
| Function / homology | Function and homology informationUBC13-MMS2 complex / ubiquitin conjugating enzyme complex / ubiquitin-protein transferase activator activity / positive regulation of protein K63-linked ubiquitination / DNA double-strand break processing / DNA damage tolerance / Formation of the ternary complex, and subsequently, the 43S complex / E2 ubiquitin-conjugating enzyme / Ribosomal scanning and start codon recognition / positive regulation of double-strand break repair ...UBC13-MMS2 complex / ubiquitin conjugating enzyme complex / ubiquitin-protein transferase activator activity / positive regulation of protein K63-linked ubiquitination / DNA double-strand break processing / DNA damage tolerance / Formation of the ternary complex, and subsequently, the 43S complex / E2 ubiquitin-conjugating enzyme / Ribosomal scanning and start codon recognition / positive regulation of double-strand break repair / Translation initiation complex formation / SARS-CoV-1 modulates host translation machinery / ubiquitin conjugating enzyme activity / Peptide chain elongation / positive regulation of intracellular signal transduction / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / Viral mRNA Translation / protein K63-linked ubiquitination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / protein monoubiquitination / GTP hydrolysis and joining of the 60S ribosomal subunit / ubiquitin ligase complex / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / regulation of DNA repair / negative regulation of TORC1 signaling / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / antiviral innate immune response / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / cytosolic ribosome / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / Regulation of FZD by ubiquitination / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / Regulation of innate immune responses to cytosolic DNA / Pexophagy / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / VLDLR internalisation and degradation / Regulation of PTEN localization / positive regulation of DNA repair / Regulation of BACH1 activity / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by REV1 / TICAM1, RIP1-mediated IKK complex recruitment / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Josephin domain DUBs / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / IKK complex recruitment mediated by RIP1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / ubiquitin binding / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / TCF dependent signaling in response to WNT / APC/C:Cdc20 mediated degradation of Securin / Regulation of NF-kappa B signaling / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / activated TAK1 mediates p38 MAPK activation / Ubiquitin-dependent degradation of Cyclin D Similarity search - Function | ||||||
| Biological species | ![]() Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.39 Å | ||||||
Authors | Wang, Y. / Huang, Y. / Chang, M. / Feng, Y. | ||||||
| Funding support | China, 1items
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Citation | Journal: Nat Commun / Year: 2020Title: Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC. Authors: Mu, Y. / Wang, Y. / Huang, Y. / Li, D. / Han, Y. / Chang, M. / Fu, J. / Xie, Y. / Ren, J. / Wang, H. / Zhang, Y. / Luo, Z.Q. / Feng, Y. | ||||||
| History |
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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 | 6kg6.cif.gz | 139.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6kg6.ent.gz | 105.7 KB | Display | PDB format |
| PDBx/mmJSON format | 6kg6.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kg/6kg6 ftp://data.pdbj.org/pub/pdb/validation_reports/kg/6kg6 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 6k3bC ![]() 6kfpC ![]() 1j7dS ![]() 1ubqS ![]() 5tscS 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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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 43532.133 Da / Num. of mol.: 1 / Mutation: C74A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Protein | Mass: 8859.106 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RPS27A / Production host: ![]() |
| #3: Protein | Mass: 17157.770 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2N, BLU / Production host: ![]() References: UniProt: P61088, E2 ubiquitin-conjugating enzyme |
| #4: 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: 2.71 Å3/Da / Density % sol: 54.67 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: PEG 4000, Tris |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.979 Å |
| Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 18, 2019 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
| Reflection | Resolution: 2.39→50 Å / Num. obs: 29359 / % possible obs: 99.56 % / Redundancy: 6.1 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 22.6 |
| Reflection shell | Resolution: 2.39→2.48 Å / Rmerge(I) obs: 0.325 / Num. unique obs: 2853 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 5TSC, 1J7D, 1UBQ Resolution: 2.39→30.94 Å / Cross valid method: FREE R-VALUE
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| Refinement step | Cycle: LAST / Resolution: 2.39→30.94 Å
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| LS refinement shell | Resolution: 2.391→2.477 Å
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About Yorodumi





Homo sapiens (human)
X-RAY DIFFRACTION
China, 1items
Citation














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