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Yorodumi- PDB-2egm: Solution structure of the zf-B_box domain from human Tripartite m... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2egm | ||||||
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Title | Solution structure of the zf-B_box domain from human Tripartite motif protein 41 | ||||||
Components | Tripartite motif-containing protein 41 | ||||||
Keywords | TRANSCRIPTION/METAL BINDING PROTEIN / zf-B_box domain / Tripartite motif protein 41 / TRIM41 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI / TRANSCRIPTION-METAL BINDING PROTEIN COMPLEX | ||||||
Function / homology | Function and homology information cellular response to muramyl dipeptide / positive regulation of type I interferon-mediated signaling pathway / protein monoubiquitination / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / cellular response to lipopolysaccharide / defense response to virus / nuclear body / protein ubiquitination ...cellular response to muramyl dipeptide / positive regulation of type I interferon-mediated signaling pathway / protein monoubiquitination / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / cellular response to lipopolysaccharide / defense response to virus / nuclear body / protein ubiquitination / nucleolus / zinc ion binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Inoue, K. / Nagashima, T. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the zf-B_box domain from human Tripartite motif protein 41 Authors: Inoue, K. / Nagashima, T. / Hayashi, F. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2egm.cif.gz | 331 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2egm.ent.gz | 275.4 KB | Display | PDB format |
PDBx/mmJSON format | 2egm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2egm_validation.pdf.gz | 343 KB | Display | wwPDB validaton report |
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Full document | 2egm_full_validation.pdf.gz | 454.9 KB | Display | |
Data in XML | 2egm_validation.xml.gz | 19.8 KB | Display | |
Data in CIF | 2egm_validation.cif.gz | 31.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eg/2egm ftp://data.pdbj.org/pub/pdb/validation_reports/eg/2egm | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 6103.860 Da / Num. of mol.: 1 / Fragment: zf-B_box domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: TRIM41 / Plasmid: P060508-23 / References: UniProt: Q8WV44 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.71mM U-15N,13C-labeled protein; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 0.05mM ZnCl2+1mM IDA; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy,target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |